The Interaction Between Ribosomal Protein S8 and Its Binding Sites on 16S RRNA and Spc MRNA & the Minimum Structural Elements of 23S RRNA Required for Binding with Ribosomal Protein L1 PDF Download
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Author: Lihong Jiang
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 172
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Book Description
Author: Lihong Jiang
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 172
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Book Description
Author:
Publisher:
ISBN:
Category : Medicine
Languages : en
Pages : 1416
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Book Description
Author: Irina V. Alimova
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 176
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Book Description
Author:
Publisher:
ISBN:
Category : Nucleic acids
Languages : en
Pages : 1288
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Book Description
Author: Danesh Moazed
Publisher:
ISBN:
Category : Ligands
Languages : en
Pages : 394
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Book Description
Author: Marina V. Rodnina
Publisher: Springer Science & Business Media
ISBN: 3709102154
Category : Medical
Languages : en
Pages : 428
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Book Description
The ribosome is a macromolecular machine that synthesizes proteins with a high degree of speed and accuracy. Our present understanding of its structure, function and dynamics is the result of six decades of research. This book collects over 40 articles based on the talks presented at the 2010 Ribosome Meeting, held in Orvieto, Italy, covering all facets of the structure and function of the ribosome. New high-resolution crystal structures of functional ribosome complexes and cryo-EM structures of translating ribosomes are presented, while partial reactions of translation are examined in structural and mechanistic detail, featuring translocation as a most dynamic process. Mechanisms of initiation, both in bacterial and eukaryotic systems, translation termination, and novel details of the functions of the respective factors are described. Structure and interactions of the nascent peptide within, and emerging from, the ribosomal peptide exit tunnel are addressed in several articles. Structural and single-molecule studies reveal a picture of the ribosome exhibiting the energy landscape of a processive Brownian machine. The collection provides up-to-date reviews which will serve as a source of essential information for years to come.
Author: Veysel Berk
Publisher:
ISBN:
Category :
Languages : en
Pages : 316
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Book Description
Author: Raymond R. Samaha
Publisher:
ISBN:
Category : RNA.
Languages : en
Pages : 308
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Book Description
Author: Albert Theodore Powers
Publisher:
ISBN:
Category : RNA.
Languages : en
Pages : 334
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Book Description
Author: Deepika S. Calidas
Publisher:
ISBN:
Category :
Languages : en
Pages : 136
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Book Description
"The function of the small subunit (SSU) of the ribosome of Escherichia coli is dependent on dynamic interactions at the intersection of its four domains; namely, the body, platform, head and penultimate stem. The in vitro assembly of each individual domain from its corresponding structural element in 16S ribosomal RNA (rRNA), i.e., the 5', central, 3' major and minor domains and associated ribosomal proteins (r-proteins) has been extensively researched. Less is understood of the long range interactions that occur during assembly as different domains co-assemble, both in vitro and in vivo. Our first approach was to use directed probing from the S8 r-protein as a monitor of SSU assembly. We found that assembly of the neck, a functionally significant region between the head and platform is dependent on assembly of the body. Furthermore, S8 binds two distinct binding sites in 16S rRNA separated by several hundred nucleotides, and the appropriate architecture of the later transcribed region is dependent upon incorporation of r-proteins to the earlier transcribed region. Elements of the body domain, including the 5' terminus do not assume their appropriate conformation except upon assembly of the entire domain. Also, we found that S12 could influence the architecture of the 5' terminus, leading us to examine the role of S12 in 30S subunit assembly, both in vitro and in vivo. S12 possesses a non-canonically structured extension that extends from the solvent surface to the intersubunit surface of the SSU, contacting multiple domains. An almost complete truncation of the extension was unable to support growth, while partial truncations of more than 6 amino acids exhibited growth defects. Truncation of half or all of the extension also resulted in reduced activity of SSUs assembled in vitro. The architecture of ribonucleoprotein complexes assembled with truncated proteins is also altered. The work presented in this thesis elucidates influence of widely separated elements of the SSU on each other during assembly"--Page v.
