Eukaryotic initiation factor: Difference between revisions
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{{Short description|Protein involved in gene expression}} |
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{{Refimprove|date=December 2014}}'''Eukaryotic initiation factors''' ('''eIFs''') are proteins involved in the initiation phase of [[eukaryotic translation]]. |
{{Refimprove|date=December 2014}}'''Eukaryotic initiation factors''' ('''eIFs''') are [[Protein|proteins]] or [[Protein complex|protein complexes]] involved in the initiation phase of [[eukaryotic translation]]. These proteins help stabilize the formation of ribosomal preinitiation complexes around the start [[codon]] and are an important input for [[Post-transcriptional regulation|post-transcription gene regulation]]. Several [[initiation factor]]s form a complex with the small [[40S]] ribosomal subunit and Met-[[tRNA]]<sub>i</sub><sup>Met</sup> called the [[43S preinitiation complex]] (43S PIC). Additional factors of the [[eIF4F]] complex (eIF4A, E, and G) recruit the 43S PIC to the [[five-prime cap]] structure of the [[mRNA]], from which the 43S particle scans 5'-->3' along the mRNA to reach an AUG start codon. Recognition of the start codon by the Met-tRNA<sub>i</sub><sup>Met</sup> promotes gated phosphate and [[eIF1]] release to form the [[48S preinitiation complex]] (48S PIC), followed by large [[60S]] ribosomal subunit recruitment to form the [[Eukaryotic ribosome (80S)|80S ribosome]].<ref name=jackson2010>{{cite journal | vauthors = Jackson RJ, Hellen CU, Pestova TV | title = The mechanism of eukaryotic translation initiation and principles of its regulation | journal = Nature Reviews Molecular Cell Biology | volume = 11 | issue = 2 | pages = 113–27 | date = February 2010 | pmid = 20094052 | pmc = 4461372 | doi = 10.1038/nrm2838 }}</ref> There exist many more eukaryotic initiation factors than [[prokaryotic initiation factors]], reflecting the greater biological complexity of eukaryotic translation. There are at least twelve eukaryotic initiation factors, composed of many more polypeptides, and these are described below.<ref name="Aitken">{{cite journal | vauthors = Aitken CE, Lorsch JR | title = A mechanistic overview of translation initiation in eukaryotes | journal = Nature Structural & Molecular Biology | volume = 19 | issue = 6 | pages = 568–76 | date = June 2012 | pmid = 22664984 | doi = 10.1038/nsmb.2303 | s2cid = 9201095 }}</ref> |
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== eIF1 |
== eIF1 and eIF1A == |
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[[eIF1]] and [[EIF1AX|eIF1A]] both bind to the 40S ribosome subunit-mRNA complex. Together they induce an "open" conformation of the mRNA binding channel, which is crucial for scanning, tRNA delivery, and start codon recognition.<ref name="Passmore">{{cite journal| |
[[eIF1]] and [[EIF1AX|eIF1A]] both bind to the 40S ribosome subunit-mRNA complex. Together they induce an "open" conformation of the mRNA binding channel, which is crucial for scanning, tRNA delivery, and start codon recognition.<ref name="Passmore">{{cite journal | vauthors = Passmore LA, Schmeing TM, Maag D, Applefield DJ, Acker MG, Algire MA, Lorsch JR, Ramakrishnan V | title = The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome | journal = Molecular Cell | volume = 26 | issue = 1 | pages = 41–50 | date = April 2007 | pmid = 17434125 | doi = 10.1016/j.molcel.2007.03.018 | doi-access = free }}</ref> In particular, eIF1 dissociation from the 40S subunit is considered to be a key step in start codon recognition.<ref name="Yuen-Nei">{{cite journal | vauthors = Cheung YN, Maag D, Mitchell SF, Fekete CA, Algire MA, Takacs JE, Shirokikh N, Pestova T, Lorsch JR, Hinnebusch AG | title = Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo | journal = Genes & Development | volume = 21 | issue = 10 | pages = 1217–30 | date = May 2007 | pmid = 17504939 | pmc = 1865493 | doi = 10.1101/gad.1528307 }}</ref> |
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| ⚫ | eIF1 and eIF1A are small proteins (13 and 16 kDa, respectively in humans) and are both components of the [[43S preinitiation complex|43S PIC]]. eIF1 binds near the ribosomal [[P-site]], while eIF1A binds near the [[A-site]], in a manner similar to the structurally and functionally related bacterial counterparts [[Prokaryotic initiation factor-1|IF3]] and [[Prokaryotic initiation factor-3|IF1]], respectively.<ref name="Fraser">{{cite journal | vauthors = Fraser CS | title = Quantitative studies of mRNA recruitment to the eukaryotic ribosome | journal = Biochimie | volume = 114 | pages = 58–71 | date = July 2015 | pmid = 25742741 | pmc = 4458453 | doi = 10.1016/j.biochi.2015.02.017 }}</ref> |
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| ⚫ | eIF1 and eIF1A are small proteins ( |
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== eIF2 == |
== eIF2 == |
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{{main article|eIF2}} |
{{main article|eIF2}} |
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eIF2 is |
eIF2 is the main protein complex responsible for delivering the initiator tRNA to the P-site of the preinitiation complex, as a ternary complex containing Met-[[tRNA]]<sub>i</sub><sup>Met</sup> and GTP (the eIF2-TC). eIF2 has specificity for the methionine-charged initiator tRNA, which is distinct from other methionine-charged tRNAs used for elongation of the polypeptide chain. The eIF2 ternary complex remains bound to the P-site while the mRNA attaches to the 40s ribosome and the complex begins to scan the mRNA. Once the AUG start codon is recognized and located in the P-site, eIF5 stimulates the hydrolysis of eIF2-GTP, effectively switching it to the [[Guanosine diphosphate|GDP]]-bound form via gated phosphate release.<ref name="Aitken">{{cite journal | vauthors = Aitken CE, Lorsch JR | title = A mechanistic overview of translation initiation in eukaryotes | journal = Nature Structural & Molecular Biology | volume = 19 | issue = 6 | pages = 568–76 | date = June 2012 | pmid = 22664984 | doi = 10.1038/nsmb.2303 | s2cid = 9201095 }}</ref> The hydrolysis of eIF2-GTP provides the conformational change to change the scanning complex into the 48S Initiation complex with the initiator tRNA-Met anticodon base paired to the AUG. After the initiation complex is formed the 60s subunit joins and eIF2 along with most of the initiation factors dissociate from the complex allowing the 60S subunit to bind. eIF1A and eIF5B-GTP remain bound to one another in the A site and must be hydrolyzed to be released and properly initiate elongation.<ref>{{Cite book|vauthors=Lodish H, Berk A, Kaiser CA, Krieger M, Bretscher A, Ploegh H, Amon A, Martin KC|title=Molecular Cell Biology|edition=8th|language=en|isbn=978-1-4641-8339-3|lccn=2015957295|year=2016|publisher=W. H. Freeman and Company|location=New York}}</ref>{{rp|191-192}} |
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eIF2 has three subunits, eIF2-[[EIF2S1|α]], [[EIF2S2|β]], and [[EIF2S3|γ]]. The former is of particular importance for cells that may need to turn off protein synthesis globally. When phosphorylated, it sequesters [[eIF2B]] (not to be confused with |
eIF2 has three subunits, eIF2-[[EIF2S1|α]], [[EIF2S2|β]], and [[EIF2S3|γ]]. The former α-subunit is a target of regulatory phosphorylation and is of particular importance for cells that may need to turn off protein synthesis globally as a response to [[cell signaling]] events. When phosphorylated, it sequesters [[eIF2B]] (not to be confused with eIF2β), a [[Guanine nucleotide exchange factor|GEF]]. Without this GEF, GDP cannot be exchanged for GTP, and translation is repressed. One example of this is the eIF2α-induced translation repression that occurs in [[reticulocytes]] when starved for iron. In the case of viral infection, [[protein kinase R]] (PKR) phosphorylates eIF2α when [[dsRNA]] is detected in many multicellular organisms, leading to cell death. |
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The proteins [[eIF2A]] and [[eIF2D]] are both technically named 'eIF2' but neither are part of the eIF2 heterotrimer and they seem to play unique functions in translation. Instead, they appear to be involved in specialized pathways, such as 'eIF2-independent' translation initiation or re-initiation, respectively. |
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eIF2α-induced translation repression occurs in [[reticulocytes]] when starved for iron. In addition, [[protein kinase R]] (PKR) phosphorylates eIF2α when [[dsRNA]] is detected in many multicellular organisms, leading to cell death. |
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== eIF3 == |
== eIF3 == |
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{{main article|eIF3}} |
{{main article|eIF3}} |
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[[Eukaryotic initiation factor 3|eIF3]] independently binds the [[40S]] ribosomal subunit, multiple initiation factors, and cellular and viral mRNA.<ref name="Hinnebusch">{{ |
[[Eukaryotic initiation factor 3|eIF3]] independently binds the [[40S]] ribosomal subunit, multiple initiation factors, and cellular and viral mRNA.<ref name="Hinnebusch">{{cite journal | vauthors = Hinnebusch AG | title = eIF3: a versatile scaffold for translation initiation complexes | language = en | journal = Trends in Biochemical Sciences | volume = 31 | issue = 10 | pages = 553–62 | date = October 2006 | pmid = 16920360 | doi = 10.1016/j.tibs.2006.08.005 }}</ref> |
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In mammals, eIF3 is the largest initiation factor, made up of 13 subunits (a-m). It has a molecular weight of ~ |
In mammals, [[eIF3]] is the largest initiation factor, made up of 13 subunits (a-m). It has a molecular weight of ~800 kDa and controls the assembly of the [[40S]] [[ribosome|ribosomal]] subunit on mRNA that have a [[five-prime cap|5' cap]] or an [[Internal ribosome entry site|IRES]]. eIF3 may use the [[eIF4F]] complex, or alternatively during internal initiation, an [[Internal ribosome entry site|IRES]], to position the mRNA strand near the exit site of the 40S ribosomal subunit, thus promoting the assembly of a functional pre-initiation complex. |
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In many human cancers, eIF3 subunits are overexpressed (subunits a, b, c, h, i, and m) and underexpressed (subunits e and f).<ref>{{ |
In many human cancers, eIF3 subunits are overexpressed (subunits a, b, c, h, i, and m) and underexpressed (subunits e and f).<ref>{{cite journal | vauthors = Hershey JW | title = The role of eIF3 and its individual subunits in cancer | journal = Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms | volume = 1849 | issue = 7 | pages = 792–800 | date = July 2015 | pmid = 25450521 | doi = 10.1016/j.bbagrm.2014.10.005 }}</ref> One potential mechanism to explain this disregulation comes from the finding that eIF3 binds a specific set of cell proliferation regulator mRNA transcripts and regulates their translation.<ref name=Lee>{{cite journal | vauthors = Lee AS, Kranzusch PJ, Cate JH | title = eIF3 targets cell-proliferation messenger RNAs for translational activation or repression | language = en | journal = Nature | volume = 522 | issue = 7554 | pages = 111–4 | date = June 2015 | pmid = 25849773 | pmc = 4603833 | doi = 10.1038/nature14267 | bibcode = 2015Natur.522..111L }}</ref> eIF3 also mediates cellular signaling through [[P70-S6 Kinase 1|S6K1]] and [[mTORC1|mTOR]]/[[RPTOR|Raptor]] to effect translational regulation.<ref name="Holz">{{cite journal | vauthors = Holz MK, Ballif BA, Gygi SP, Blenis J | title = mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events | journal = Cell | volume = 123 | issue = 4 | pages = 569–80 | date = November 2005 | pmid = 16286006 | doi = 10.1016/j.cell.2005.10.024 | doi-access = free }}</ref> |
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== |
== eIF4 == |
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{{main article|eIF4F}} |
{{main article|eIF4F}} |
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eIF4B contains two RNA-binding domains{{spaced ndash}}one non-specifically interacts with mRNA, whereas the second specifically binds the 18S portion of the small ribosomal subunit. It acts as an anchor, as well as a critical co-factor for eIF4A. It is also a substrate of S6K, and when phosphorylated, it promotes the formation of the pre-initiation complex. In vertebrates, eIF4H is an additional initiation factor with similar function to eIF4B. |
eIF4B contains two RNA-binding domains{{spaced ndash}}one non-specifically interacts with mRNA, whereas the second specifically binds the 18S portion of the small ribosomal subunit. It acts as an anchor, as well as a critical co-factor for eIF4A. It is also a substrate of S6K, and when phosphorylated, it promotes the formation of the pre-initiation complex. In vertebrates, eIF4H is an additional initiation factor with similar function to eIF4B. |
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== eIF5 |
== eIF5, eIF5A and eIF5B == |
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[[eIF5A|eIF5]] is a [[GTPase-activating protein]], which helps the large ribosomal subunit associate with the small subunit. It is required for GTP-hydrolysis by eIF2 |
[[eIF5A|eIF5]] is a [[GTPase-activating protein]], which helps the large ribosomal subunit associate with the small subunit. It is required for GTP-hydrolysis by eIF2. |
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[[ |
[[eIF5A]] is the eukaryotic homolog of [[elongation factor P|EF-P]]. It helps with elongation and also plays a role in termination. EIF5A contains the unusual amino acid [[hypusine]].<ref>{{cite journal |last1=Schuller |first1=AP |last2=Wu |first2=CC |last3=Dever |first3=TE |last4=Buskirk |first4=AR |last5=Green |first5=R |title=eIF5A Functions Globally in Translation Elongation and Termination. |journal=Molecular Cell |date=20 April 2017 |volume=66 |issue=2 |pages=194–205.e5 |doi=10.1016/j.molcel.2017.03.003 |pmid=28392174|pmc=5414311 }}</ref> |
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[[eIF5B]] is a [[GTPase]], and is involved in assembly of the full ribosome. It is the functional eukaryotic analog of bacterial [[Prokaryotic initiation factor-2|IF2]].<ref name="Allen">{{cite journal | vauthors = Allen GS, Frank J | title = Structural insights on the translation initiation complex: ghosts of a universal initiation complex | journal = Molecular Microbiology | volume = 63 | issue = 4 | pages = 941–50 | date = February 2007 | pmid = 17238926 | doi = 10.1111/j.1365-2958.2006.05574.x | doi-access = free }}</ref> |
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== eIF6 == |
== eIF6 == |
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[[eIF6]] performs the same inhibition of ribosome assembly as eIF3, but binds with the [[60S|large subunit]]. |
[[eIF6]] performs the same inhibition of ribosome assembly as eIF3, but binds with the [[60S|large subunit]]. |
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==See also== |
== See also == |
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*[[Eukaryotic translation]] |
*[[Eukaryotic translation]] |
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*[[DDX3X|Ded1/DDX3]] |
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*[[DHX29]] |
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==References== |
== References == |
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{{reflist}} |
{{reflist}} |
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== Further reading == |
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| ⚫ | |||
{{refbegin}} |
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* {{cite journal |doi=10.1038/nrmicro1558 |pmid=17128284 |year=2007 |last1=Fraser |first1=CS |last2=Doudna |first2=JA |title=Structural and mechanistic insights into hepatitis C viral translation initiation |volume=5 |issue=1 |pages=29–38 |journal=Nature Reviews Microbiology}} |
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*{{cite journal | |
* {{cite journal | vauthors = Fraser CS, Doudna JA | title = Structural and mechanistic insights into hepatitis C viral translation initiation | journal = Nature Reviews. Microbiology | volume = 5 | issue = 1 | pages = 29–38 | date = January 2007 | pmid = 17128284 | doi = 10.1038/nrmicro1558 | s2cid = 638721 }} |
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* {{cite journal | vauthors = Malys N, McCarthy JE | title = Translation initiation: variations in the mechanism can be anticipated | journal = Cellular and Molecular Life Sciences | volume = 68 | issue = 6 | pages = 991–1003 | date = March 2011 | pmid = 21076851 | doi = 10.1007/s00018-010-0588-z | s2cid = 31720000 }} |
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{{refend}} |
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| ⚫ | |||
* {{MeshName|Eukaryotic+Initiation+Factors}} |
* {{MeshName|Eukaryotic+Initiation+Factors}} |
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Revision as of 17:35, 9 July 2023
 | This article needs additional citations for verification. (December 2014) |
Eukaryotic initiation factors (eIFs) are proteins or protein complexes involved in the initiation phase of eukaryotic translation. These proteins help stabilize the formation of ribosomal preinitiation complexes around the start codon and are an important input for post-transcription gene regulation. Several initiation factors form a complex with the small 40S ribosomal subunit and Met-tRNAiMet called the 43S preinitiation complex (43S PIC). Additional factors of the eIF4F complex (eIF4A, E, and G) recruit the 43S PIC to the five-prime cap structure of the mRNA, from which the 43S particle scans 5'-->3' along the mRNA to reach an AUG start codon. Recognition of the start codon by the Met-tRNAiMet promotes gated phosphate and eIF1 release to form the 48S preinitiation complex (48S PIC), followed by large 60S ribosomal subunit recruitment to form the 80S ribosome.[1] There exist many more eukaryotic initiation factors than prokaryotic initiation factors, reflecting the greater biological complexity of eukaryotic translation. There are at least twelve eukaryotic initiation factors, composed of many more polypeptides, and these are described below.[2]
eIF1 and eIF1A
eIF1 and eIF1A both bind to the 40S ribosome subunit-mRNA complex. Together they induce an "open" conformation of the mRNA binding channel, which is crucial for scanning, tRNA delivery, and start codon recognition.[3] In particular, eIF1 dissociation from the 40S subunit is considered to be a key step in start codon recognition.[4] eIF1 and eIF1A are small proteins (13 and 16 kDa, respectively in humans) and are both components of the 43S PIC. eIF1 binds near the ribosomal P-site, while eIF1A binds near the A-site, in a manner similar to the structurally and functionally related bacterial counterparts IF3 and IF1, respectively.[5]
eIF2
eIF2 is the main protein complex responsible for delivering the initiator tRNA to the P-site of the preinitiation complex, as a ternary complex containing Met-tRNAiMet and GTP (the eIF2-TC). eIF2 has specificity for the methionine-charged initiator tRNA, which is distinct from other methionine-charged tRNAs used for elongation of the polypeptide chain. The eIF2 ternary complex remains bound to the P-site while the mRNA attaches to the 40s ribosome and the complex begins to scan the mRNA. Once the AUG start codon is recognized and located in the P-site, eIF5 stimulates the hydrolysis of eIF2-GTP, effectively switching it to the GDP-bound form via gated phosphate release.[2] The hydrolysis of eIF2-GTP provides the conformational change to change the scanning complex into the 48S Initiation complex with the initiator tRNA-Met anticodon base paired to the AUG. After the initiation complex is formed the 60s subunit joins and eIF2 along with most of the initiation factors dissociate from the complex allowing the 60S subunit to bind. eIF1A and eIF5B-GTP remain bound to one another in the A site and must be hydrolyzed to be released and properly initiate elongation.[6]: 191–192
eIF2 has three subunits, eIF2-α, β, and γ. The former α-subunit is a target of regulatory phosphorylation and is of particular importance for cells that may need to turn off protein synthesis globally as a response to cell signaling events. When phosphorylated, it sequesters eIF2B (not to be confused with eIF2β), a GEF. Without this GEF, GDP cannot be exchanged for GTP, and translation is repressed. One example of this is the eIF2α-induced translation repression that occurs in reticulocytes when starved for iron. In the case of viral infection, protein kinase R (PKR) phosphorylates eIF2α when dsRNA is detected in many multicellular organisms, leading to cell death.
The proteins eIF2A and eIF2D are both technically named 'eIF2' but neither are part of the eIF2 heterotrimer and they seem to play unique functions in translation. Instead, they appear to be involved in specialized pathways, such as 'eIF2-independent' translation initiation or re-initiation, respectively.
eIF3
eIF3 independently binds the 40S ribosomal subunit, multiple initiation factors, and cellular and viral mRNA.[7]
In mammals, eIF3 is the largest initiation factor, made up of 13 subunits (a-m). It has a molecular weight of ~800 kDa and controls the assembly of the 40S ribosomal subunit on mRNA that have a 5' cap or an IRES. eIF3 may use the eIF4F complex, or alternatively during internal initiation, an IRES, to position the mRNA strand near the exit site of the 40S ribosomal subunit, thus promoting the assembly of a functional pre-initiation complex.
In many human cancers, eIF3 subunits are overexpressed (subunits a, b, c, h, i, and m) and underexpressed (subunits e and f).[8] One potential mechanism to explain this disregulation comes from the finding that eIF3 binds a specific set of cell proliferation regulator mRNA transcripts and regulates their translation.[9] eIF3 also mediates cellular signaling through S6K1 and mTOR/Raptor to effect translational regulation.[10]
eIF4
The eIF4F complex is composed of three subunits: eIF4A, eIF4E, and eIF4G. Each subunit has multiple human isoforms and there exist additional eIF4 proteins: eIF4B and eIF4H.
eIF4G is a 175.5-kDa scaffolding protein that interacts with eIF3 and the Poly(A)-binding protein (PABP), as well as the other members of the eIF4F complex. eIF4E recognizes and binds to the 5' cap structure of mRNA, while eIF4G binds PABP, which binds the poly(A) tail, potentially circularizing and activating the bound mRNA. eIF4A – a DEAD box RNA helicase – is important for resolving mRNA secondary structures.
eIF4B contains two RNA-binding domains – one non-specifically interacts with mRNA, whereas the second specifically binds the 18S portion of the small ribosomal subunit. It acts as an anchor, as well as a critical co-factor for eIF4A. It is also a substrate of S6K, and when phosphorylated, it promotes the formation of the pre-initiation complex. In vertebrates, eIF4H is an additional initiation factor with similar function to eIF4B.
eIF5, eIF5A and eIF5B
eIF5 is a GTPase-activating protein, which helps the large ribosomal subunit associate with the small subunit. It is required for GTP-hydrolysis by eIF2.
eIF5A is the eukaryotic homolog of EF-P. It helps with elongation and also plays a role in termination. EIF5A contains the unusual amino acid hypusine.[11]
eIF5B is a GTPase, and is involved in assembly of the full ribosome. It is the functional eukaryotic analog of bacterial IF2.[12]
eIF6
eIF6 performs the same inhibition of ribosome assembly as eIF3, but binds with the large subunit.
See also
References
- ^ Jackson RJ, Hellen CU, Pestova TV (February 2010). "The mechanism of eukaryotic translation initiation and principles of its regulation". Nature Reviews Molecular Cell Biology. 11 (2): 113–27. doi:10.1038/nrm2838. PMC 4461372. PMID 20094052.
- ^ a b Aitken CE, Lorsch JR (June 2012). "A mechanistic overview of translation initiation in eukaryotes". Nature Structural & Molecular Biology. 19 (6): 568–76. doi:10.1038/nsmb.2303. PMID 22664984. S2CID 9201095.
- ^ Passmore LA, Schmeing TM, Maag D, Applefield DJ, Acker MG, Algire MA, Lorsch JR, Ramakrishnan V (April 2007). "The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome". Molecular Cell. 26 (1): 41–50. doi:10.1016/j.molcel.2007.03.018. PMID 17434125.
- ^ Cheung YN, Maag D, Mitchell SF, Fekete CA, Algire MA, Takacs JE, Shirokikh N, Pestova T, Lorsch JR, Hinnebusch AG (May 2007). "Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo". Genes & Development. 21 (10): 1217–30. doi:10.1101/gad.1528307. PMC 1865493. PMID 17504939.
- ^ Fraser CS (July 2015). "Quantitative studies of mRNA recruitment to the eukaryotic ribosome". Biochimie. 114: 58–71. doi:10.1016/j.biochi.2015.02.017. PMC 4458453. PMID 25742741.
- ^ Lodish H, Berk A, Kaiser CA, Krieger M, Bretscher A, Ploegh H, Amon A, Martin KC (2016). Molecular Cell Biology (8th ed.). New York: W. H. Freeman and Company. ISBN 978-1-4641-8339-3. LCCN 2015957295.
- ^ Hinnebusch AG (October 2006). "eIF3: a versatile scaffold for translation initiation complexes". Trends in Biochemical Sciences. 31 (10): 553–62. doi:10.1016/j.tibs.2006.08.005. PMID 16920360.
- ^ Hershey JW (July 2015). "The role of eIF3 and its individual subunits in cancer". Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms. 1849 (7): 792–800. doi:10.1016/j.bbagrm.2014.10.005. PMID 25450521.
- ^ Lee AS, Kranzusch PJ, Cate JH (June 2015). "eIF3 targets cell-proliferation messenger RNAs for translational activation or repression". Nature. 522 (7554): 111–4. Bibcode:2015Natur.522..111L. doi:10.1038/nature14267. PMC 4603833. PMID 25849773.
- ^ Holz MK, Ballif BA, Gygi SP, Blenis J (November 2005). "mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events". Cell. 123 (4): 569–80. doi:10.1016/j.cell.2005.10.024. PMID 16286006.
- ^ Schuller, AP; Wu, CC; Dever, TE; Buskirk, AR; Green, R (20 April 2017). "eIF5A Functions Globally in Translation Elongation and Termination". Molecular Cell. 66 (2): 194–205.e5. doi:10.1016/j.molcel.2017.03.003. PMC 5414311. PMID 28392174.
- ^ Allen GS, Frank J (February 2007). "Structural insights on the translation initiation complex: ghosts of a universal initiation complex". Molecular Microbiology. 63 (4): 941–50. doi:10.1111/j.1365-2958.2006.05574.x. PMID 17238926.
Further reading
- Fraser CS, Doudna JA (January 2007). "Structural and mechanistic insights into hepatitis C viral translation initiation". Nature Reviews. Microbiology. 5 (1): 29–38. doi:10.1038/nrmicro1558. PMID 17128284. S2CID 638721.
- Malys N, McCarthy JE (March 2011). "Translation initiation: variations in the mechanism can be anticipated". Cellular and Molecular Life Sciences. 68 (6): 991–1003. doi:10.1007/s00018-010-0588-z. PMID 21076851. S2CID 31720000.
External links
- Eukaryotic+Initiation+Factors at the U.S. National Library of Medicine Medical Subject Headings (MeSH)