Mechanism of eIF6-mediated inhibition of ribosomal subunit joining

Marco Gartmann; Michael Blau; Jean Paul Armache; Thorsten Mielke; Maya Topf; Roland Beckmann

doi:10.1074/jbc.C109.096057

Mechanism of eIF6-mediated inhibition of ribosomal subunit joining

Marco Gartmann, Michael Blau, Jean Paul Armache, Thorsten Mielke, Maya Topf, Roland Beckmann

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

99 Scopus citations

Abstract

During the process of ribosomal assembly, the essential eukaryotic translation initiation factor 6 (eIF6) is known to act as a ribosomal anti-association factor. However, a molecular understanding of the anti-association activity of eIF6 is still missing. Here we present the cryo-electron microscopy reconstruction of a complex of the large ribosomal subunit with eukaryotic eIF6 from Saccharomyces cerevisiae. The structure reveals that the eIF6 binding site involves mainly rpL23 (L14p in Escherichia coli). Based on our structural data, we propose that the mechanism of the anti-association activity of eIF6 is based on steric hindrance of intersubunit bridge formation around the dynamic bridge B6.

Original language	English (US)
Pages (from-to)	14848-14851
Number of pages	4
Journal	Journal of Biological Chemistry
Volume	285
Issue number	20
DOIs	https://doi.org/10.1074/jbc.C109.096057
State	Published - May 14 2010

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1074/jbc.C109.096057

Cite this

@article{df15ea54a9f8464b97e1fa8b1ebe4561,

title = "Mechanism of eIF6-mediated inhibition of ribosomal subunit joining",

abstract = "During the process of ribosomal assembly, the essential eukaryotic translation initiation factor 6 (eIF6) is known to act as a ribosomal anti-association factor. However, a molecular understanding of the anti-association activity of eIF6 is still missing. Here we present the cryo-electron microscopy reconstruction of a complex of the large ribosomal subunit with eukaryotic eIF6 from Saccharomyces cerevisiae. The structure reveals that the eIF6 binding site involves mainly rpL23 (L14p in Escherichia coli). Based on our structural data, we propose that the mechanism of the anti-association activity of eIF6 is based on steric hindrance of intersubunit bridge formation around the dynamic bridge B6.",

author = "Marco Gartmann and Michael Blau and Armache, {Jean Paul} and Thorsten Mielke and Maya Topf and Roland Beckmann",

year = "2010",

month = may,

day = "14",

doi = "10.1074/jbc.C109.096057",

language = "English (US)",

volume = "285",

pages = "14848--14851",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "20",

}

TY - JOUR

T1 - Mechanism of eIF6-mediated inhibition of ribosomal subunit joining

AU - Gartmann, Marco

AU - Blau, Michael

AU - Armache, Jean Paul

AU - Mielke, Thorsten

AU - Topf, Maya

AU - Beckmann, Roland

PY - 2010/5/14

Y1 - 2010/5/14

N2 - During the process of ribosomal assembly, the essential eukaryotic translation initiation factor 6 (eIF6) is known to act as a ribosomal anti-association factor. However, a molecular understanding of the anti-association activity of eIF6 is still missing. Here we present the cryo-electron microscopy reconstruction of a complex of the large ribosomal subunit with eukaryotic eIF6 from Saccharomyces cerevisiae. The structure reveals that the eIF6 binding site involves mainly rpL23 (L14p in Escherichia coli). Based on our structural data, we propose that the mechanism of the anti-association activity of eIF6 is based on steric hindrance of intersubunit bridge formation around the dynamic bridge B6.

AB - During the process of ribosomal assembly, the essential eukaryotic translation initiation factor 6 (eIF6) is known to act as a ribosomal anti-association factor. However, a molecular understanding of the anti-association activity of eIF6 is still missing. Here we present the cryo-electron microscopy reconstruction of a complex of the large ribosomal subunit with eukaryotic eIF6 from Saccharomyces cerevisiae. The structure reveals that the eIF6 binding site involves mainly rpL23 (L14p in Escherichia coli). Based on our structural data, we propose that the mechanism of the anti-association activity of eIF6 is based on steric hindrance of intersubunit bridge formation around the dynamic bridge B6.

UR - http://www.scopus.com/inward/record.url?scp=77952088979&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77952088979&partnerID=8YFLogxK

U2 - 10.1074/jbc.C109.096057

DO - 10.1074/jbc.C109.096057

M3 - Article

C2 - 20356839

AN - SCOPUS:77952088979

SN - 0021-9258

VL - 285

SP - 14848

EP - 14851

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 20

ER -

Mechanism of eIF6-mediated inhibition of ribosomal subunit joining

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this