期刊
MOLECULAR & CELLULAR PROTEOMICS
卷 11, 期 12, 页码 1965-1976出版社
ELSEVIER
DOI: 10.1074/mcp.M112.019562
关键词
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资金
- National Science Foundation [CHE-1012855, CHE-0832651]
- Wellcome Trust [084229, 077707, 092076]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0832651] Funding Source: National Science Foundation
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1012855] Funding Source: National Science Foundation
Ribosomal protein S1 has been shown to be a significant effector of prokaryotic translation. The protein is in fact capable of efficiently initiating translation, regardless of the presence of a Shine-Dalgarno sequence in mRNA. Structural insights into this process have remained elusive, as S1 is recalcitrant to traditional techniques of structural analysis, such as x-ray crystallography. Through the application of protein cross-linking and high resolution mass spectrometry, we have detailed the ribosomal binding site of S1 and have observed evidence of its dynamics. Our results support a previous hypothesis that S1 acts as the mRNA catching arm of the prokaryotic ribosome. We also demonstrate that in solution the major domains of the 30S subunit are remarkably flexible, capable of moving 30-50 angstrom with respect to one another. Molecular & Cellular Proteomics 11: 10.1074/mcp.M112.019562, 1965-1976, 2012.
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