Factor-dependent processivity in human eIF4A DEAD-box helicase

Cuauhtémoc García-García, Kirsten L. Frieda, Kateryna Feoktistova, Christopher S. Fraser, Steven M. Block

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

During eukaryotic translation initiation, the small ribosomal subunit, assisted by initiation factors, locates the messenger RNA start codon by scanning from the 5′ cap. This process is powered by the eukaryotic initiation factor 4A (eIF4A), a DEAD-box helicase. eIF4A has been thought to unwind structures formed in the untranslated 5′ region via a nonprocessive mechanism. Using a single-molecule assay, we found that eIF4A functions instead as an adenosine triphosphate-dependent processive helicase when complexed with two accessory proteins, eIF4G and eIF4B. Translocation occurred in discrete steps of 11 ± 2 base pairs, irrespective of the accessory factor combination. Our findings support a memory-less stepwise mechanism for translation initiation and suggest that similar factor-dependent processivity may be shared by other members of the DEAD-box helicase family.

Original languageEnglish (US)
Pages (from-to)1486-1488
Number of pages3
JournalScience
Volume348
Issue number6242
DOIs
StatePublished - Jun 26 2015

Fingerprint

Eukaryotic Initiation Factor-4A
Small Ribosome Subunits
Peptide Initiation Factors
Initiator Codon
5' Untranslated Regions
Base Pairing
Adenosine Triphosphate
Messenger RNA
Proteins

ASJC Scopus subject areas

  • General

Cite this

García-García, C., Frieda, K. L., Feoktistova, K., Fraser, C. S., & Block, S. M. (2015). Factor-dependent processivity in human eIF4A DEAD-box helicase. Science, 348(6242), 1486-1488. https://doi.org/10.1126/science.aaa5089

Factor-dependent processivity in human eIF4A DEAD-box helicase. / García-García, Cuauhtémoc; Frieda, Kirsten L.; Feoktistova, Kateryna; Fraser, Christopher S.; Block, Steven M.

In: Science, Vol. 348, No. 6242, 26.06.2015, p. 1486-1488.

Research output: Contribution to journalArticle

García-García, C, Frieda, KL, Feoktistova, K, Fraser, CS & Block, SM 2015, 'Factor-dependent processivity in human eIF4A DEAD-box helicase', Science, vol. 348, no. 6242, pp. 1486-1488. https://doi.org/10.1126/science.aaa5089
García-García C, Frieda KL, Feoktistova K, Fraser CS, Block SM. Factor-dependent processivity in human eIF4A DEAD-box helicase. Science. 2015 Jun 26;348(6242):1486-1488. https://doi.org/10.1126/science.aaa5089
García-García, Cuauhtémoc ; Frieda, Kirsten L. ; Feoktistova, Kateryna ; Fraser, Christopher S. ; Block, Steven M. / Factor-dependent processivity in human eIF4A DEAD-box helicase. In: Science. 2015 ; Vol. 348, No. 6242. pp. 1486-1488.
@article{1e37891a1bfe4211b50bde43300295a0,
title = "Factor-dependent processivity in human eIF4A DEAD-box helicase",
abstract = "During eukaryotic translation initiation, the small ribosomal subunit, assisted by initiation factors, locates the messenger RNA start codon by scanning from the 5′ cap. This process is powered by the eukaryotic initiation factor 4A (eIF4A), a DEAD-box helicase. eIF4A has been thought to unwind structures formed in the untranslated 5′ region via a nonprocessive mechanism. Using a single-molecule assay, we found that eIF4A functions instead as an adenosine triphosphate-dependent processive helicase when complexed with two accessory proteins, eIF4G and eIF4B. Translocation occurred in discrete steps of 11 ± 2 base pairs, irrespective of the accessory factor combination. Our findings support a memory-less stepwise mechanism for translation initiation and suggest that similar factor-dependent processivity may be shared by other members of the DEAD-box helicase family.",
author = "Cuauht{\'e}moc Garc{\'i}a-Garc{\'i}a and Frieda, {Kirsten L.} and Kateryna Feoktistova and Fraser, {Christopher S.} and Block, {Steven M.}",
year = "2015",
month = "6",
day = "26",
doi = "10.1126/science.aaa5089",
language = "English (US)",
volume = "348",
pages = "1486--1488",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6242",

}

TY - JOUR

T1 - Factor-dependent processivity in human eIF4A DEAD-box helicase

AU - García-García, Cuauhtémoc

AU - Frieda, Kirsten L.

AU - Feoktistova, Kateryna

AU - Fraser, Christopher S.

AU - Block, Steven M.

PY - 2015/6/26

Y1 - 2015/6/26

N2 - During eukaryotic translation initiation, the small ribosomal subunit, assisted by initiation factors, locates the messenger RNA start codon by scanning from the 5′ cap. This process is powered by the eukaryotic initiation factor 4A (eIF4A), a DEAD-box helicase. eIF4A has been thought to unwind structures formed in the untranslated 5′ region via a nonprocessive mechanism. Using a single-molecule assay, we found that eIF4A functions instead as an adenosine triphosphate-dependent processive helicase when complexed with two accessory proteins, eIF4G and eIF4B. Translocation occurred in discrete steps of 11 ± 2 base pairs, irrespective of the accessory factor combination. Our findings support a memory-less stepwise mechanism for translation initiation and suggest that similar factor-dependent processivity may be shared by other members of the DEAD-box helicase family.

AB - During eukaryotic translation initiation, the small ribosomal subunit, assisted by initiation factors, locates the messenger RNA start codon by scanning from the 5′ cap. This process is powered by the eukaryotic initiation factor 4A (eIF4A), a DEAD-box helicase. eIF4A has been thought to unwind structures formed in the untranslated 5′ region via a nonprocessive mechanism. Using a single-molecule assay, we found that eIF4A functions instead as an adenosine triphosphate-dependent processive helicase when complexed with two accessory proteins, eIF4G and eIF4B. Translocation occurred in discrete steps of 11 ± 2 base pairs, irrespective of the accessory factor combination. Our findings support a memory-less stepwise mechanism for translation initiation and suggest that similar factor-dependent processivity may be shared by other members of the DEAD-box helicase family.

UR - http://www.scopus.com/inward/record.url?scp=84933567353&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84933567353&partnerID=8YFLogxK

U2 - 10.1126/science.aaa5089

DO - 10.1126/science.aaa5089

M3 - Article

C2 - 26113725

AN - SCOPUS:84933567353

VL - 348

SP - 1486

EP - 1488

JO - Science

JF - Science

SN - 0036-8075

IS - 6242

ER -