Author: Brooke Cameron Donly
Publisher:
ISBN:
Category :
Languages : en
Pages : 318

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Author: Brooke Cameron Donly
Publisher:
ISBN:
Category : RNA.
Languages : en
Pages : 0

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Author: Marina V. Rodnina
Publisher: Springer Science & Business Media
ISBN: 3709102154
Category : Medical
Languages : en
Pages : 428

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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: Zhili Xu
Publisher:
ISBN:
Category :
Languages : en
Pages : 402

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"Ribonucleic acids (RNAs) perform widely different biological functions ranging from regulation of gene expression to catalysis. Their functions are often tightly correlated with their structure. To explore the relationship between RNA structure and function, Escherichia coli (E. coli) small ribosomal subunit was used as a model system and its biogenesis was investigated using two different approaches. Firstly, we studied a RNA modification system which involves dimethylation of two universally conserved adjacent adenosines in the ultimate helix of the small subunit ribosomal RNAs (rRNA) and the KsgA (E. coli) methyltransferase family, enzyme responsible for these two dimethylations, which also appears to be universally conserved. We localized the position of KsgA relative to 30S subunits using directed hydroxyl radical probing and demonstrated that binding of KsgA and translation initiation factor 3 (IF3) are generally mutually exclusive. Our work strongly suggested that this modification system plays a critical role in differentiating fully assembled, functional subunits from those that are still involved in the biogenesis pathway. Secondly, we devised a modification interference approach to investigate nucleotides within 16S rRNA that are potentially important for the assembly of functional 30S subunits. We found that the majority of these nucleotides are located in the head and interdomain junction of the 30S subunit indicating that the different domains of the 30S subunit assemble differentially and that the assembly of the 3' domain and interdomain junction are more restricted than assembly of the other domains. Further in vivo investigation of individual residues identified in vitro delineated the importance of these residues in ribosome biogenesis. Overall, this dissertation has demonstrated the impact of 16S rRNA structural changes on biogenesis of the small ribosomal subunit and has enabled deeper understanding of ribosome assembly."--Leaves v-vi.

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: Richard C. Conrad
Publisher:
ISBN:
Category :
Languages : en
Pages : 464

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Author: Hae Yeong Kim
Publisher:
ISBN:
Category :
Languages : en
Pages : 232

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Author: Eleanor Spicer Ward
Publisher:
ISBN:
Category : Ribosomes
Languages : en
Pages : 468

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Author: Wayne E. Taylor
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 174

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Author: John Walker Roberts
Publisher:
ISBN:
Category : Escherichia coli
Languages : en
Pages : 228

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