Studies on the Specific Interaction of Ribosomal Protein S8 from Escherichia Coli with Its Binding Site in 16S RRNA PDF Download
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Author: Irina V. Alimova
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 176
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Author: Irina V. Alimova
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 176
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Author: Lihong Jiang
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 172
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Author: Steven R. King
Publisher:
ISBN:
Category : Binding sites (Biochemistry)
Languages : en
Pages : 126
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Author: Danesh Moazed
Publisher:
ISBN:
Category : Ligands
Languages : en
Pages : 394
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Book Description
![Ribosomal RNA-protein Interactions in Escherichia Coli [microform] : Binding of Ribosomal Protein S20 to 16 S RRNA and Processing of 5 S RRNA by Ribonuclease E PDF](https://books.google.com/books/content/images/frontcover/vpPDwQEACAAJ?fife=w80-h100)
Author: Robert Stephen Cormack
Publisher: National Library of Canada = Bibliothèque nationale du Canada
ISBN: 9780315905795
Category :
Languages : en
Pages : 224
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The role of the polypeptide encoded by ams/rne/hmp1, a gene required for RNase E activity, was investigated. Northwestern blotting and UV crosslinking of substrate RNA to crude fractions containing RNase E unambiguously showed that overexpressed Ams/Rne/Hmp1 polypeptide has a high affinity for RNA. Our results demonstrate that the ams/rne/hmp1 gene product intimately associates with RNase E substrate RNA and supports the notion that Ams/Rne/Hmp1 is the nuclease responsible for RNase E activity. In addition, the RNA-binding domain of Ams/Rne/Hmp1 was localized and a putative RNase E-associated protein was identified.
Author: Robert Stephen Cormack
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 0
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Author: Deepika S. Calidas
Publisher:
ISBN:
Category :
Languages : en
Pages : 136
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"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.
Author:
Publisher:
ISBN:
Category : Medicine
Languages : en
Pages : 1844
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Author: Richard C. Conrad
Publisher:
ISBN:
Category :
Languages : en
Pages : 464
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Author: Chu Chang
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 488
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