Publikationsdatum:
2011-08-13
Beschreibung:
Ribosome assembly in eukaryotes requires approximately 200 essential assembly factors (AFs) and occurs through ordered events that initiate in the nucleolus and culminate in the cytoplasm. Here, we present the electron cryo-microscopy (cryo-EM) structure of a late cytoplasmic 40S ribosome assembly intermediate from Saccharomyces cerevisiae at 18 angstrom resolution. We obtained cryo-EM reconstructions of preribosomal complexes lacking individual components to define the positions of all seven AFs bound to this intermediate. These late-binding AFs are positioned to prevent each step in the translation initiation pathway. Together, they obstruct the binding sites for initiation factors, prevent the opening of the messenger RNA channel, block 60S subunit joining, and disrupt the decoding site. These redundant mechanisms probably ensure that pre-40S particles do not enter the translation pathway, which would result in their rapid degradation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3402165/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3402165/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strunk, Bethany S -- Loucks, Cherisse R -- Su, Min -- Vashisth, Harish -- Cheng, Shanshan -- Schilling, Justin -- Brooks, Charles L 3rd -- Karbstein, Katrin -- Skiniotis, Georgios -- P41 RR012255/RR/NCRR NIH HHS/ -- R01 GM086451/GM/NIGMS NIH HHS/ -- R01-GM086451/GM/NIGMS NIH HHS/ -- RR12255/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2011 Sep 9;333(6048):1449-53. doi: 10.1126/science.1208245. Epub 2011 Aug 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemical Biology Doctoral Program, University of Michigan, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21835981" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Binding Sites
;
Cryoelectron Microscopy
;
Eukaryotic Initiation Factor-1/chemistry/metabolism
;
Eukaryotic Initiation Factor-3/chemistry/metabolism
;
Image Processing, Computer-Assisted
;
Methyltransferases/chemistry/metabolism
;
Models, Molecular
;
Nuclear Proteins/chemistry/metabolism
;
*Peptide Chain Initiation, Translational
;
Protein-Serine-Threonine Kinases/chemistry/metabolism
;
RNA, Fungal/genetics/metabolism
;
RNA, Messenger/genetics/metabolism
;
Ribosomal Proteins/chemistry/metabolism
;
Ribosome Subunits, Small, Eukaryotic/chemistry/*metabolism/ultrastructure
;
Saccharomyces cerevisiae/chemistry/*genetics/metabolism
;
Saccharomyces cerevisiae Proteins/*chemistry/*metabolism
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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