The Study of Nuclear Ribonuclease P in S. Cerevisiae Using Novel RNA Affinity Tags PDF Download
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Author: Chatchawan Srisawat
Publisher:
ISBN:
Category :
Languages : en
Pages : 266
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Book Description
Author: Chatchawan Srisawat
Publisher:
ISBN:
Category :
Languages : en
Pages : 266
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Book Description
Author: Joel Ranier Chamberlain
Publisher:
ISBN:
Category :
Languages : en
Pages : 348
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Book Description
Author: Fenyong Liu
Publisher: Springer Science & Business Media
ISBN: 1441911421
Category : Science
Languages : en
Pages : 293
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Book Description
The Discovery of Ribonuclease P and Enzymatic Activity of Its RNA Subunit Sydney Brenner and Francis H. C. Crick had a specific project in mind when they offered Sidney Altman a position in their group in 1969 to conduct postdoctoral research at the Medical Research Council Laboratory of Molecular Biology (LMB) in Cambridge, England. At the time, an intense international competition was on- ing in as many as a dozen labs to determine the three-dimensional structure of tRNA. At the LMB, Aaron Klug was attacking the structure by crystallographic analysis with Brian F. C. Clark providing large amounts of purified phenylalanine tRNA. (Eventually, Aaron announced his empirically determined 3-D structure of yeast phenylalanine tRNA, a structure that is generally common to tRNAs, due in part to several conserved, novel three-way nucleotide interactions. ) Concurrently, Michael Levitt, a Ph. D. student of Francis, was visually scrutinizing the cloverleaf secondary structure of the 14 tRNA sequences known at the time. Levitt was searching for nucleotide covariation in different parts of the molecules that were conserved in the 14 sequences known at the time. He identified a possible covariation of an apparent Watson-Crick pairing type between the residues at position 15 from the 5’ end of the tRNA and residue 48. This association implied these parts of the tRNA, namely the D loop containing residue 15 and the 5’ end of the T stem-adjoining residue 48, folded on one another in a tertiary structure shared by different tRNAs.
Author: Anthony John Tranguch
Publisher:
ISBN:
Category :
Languages : en
Pages : 280
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Author: JAE-YONG LEE
Publisher:
ISBN:
Category :
Languages : en
Pages : 144
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Book Description
Mg$\sp{++}$ is associated with RNase P to constitute an active enzyme and that the protein subunits of S. cerevisiae nuclear RNase P may be involved in catalysis.
Author:
Publisher:
ISBN:
Category : Dissertations, Academic
Languages : en
Pages : 942
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Author:
Publisher:
ISBN:
Category : Nucleoproteins
Languages : en
Pages :
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Abstract: Ribonuclease P (RNase P) is a ribonucleoprotein involved in tRNA biosynthesis in all living organisms. Bacterial RNase P is comprised of a catalytic RNA subunit and a lone protein cofactor which plays a supporting, albeit essential, role in the tRNA processing reaction in vivo. In this study, we have searched various databases to identify homologs of the protein subunit of RNase P from diverse bacteria and generated an alignment of their primary sequences to determine the most highly conserved residues. Such an approach has helped us to extend earlier predictions of which residues might play an important role in RNase P catalysis. The amino acid residues identified as important for RNase P catalysis could be categorized in three groups: (i) the RNR motif in helix alpha 2, (ii) the substrate binding cleft, and (iii) amino acid residues involved in the overall stability of the bacterial RNase P protein subunit. By employing site-directed mutagenesis and a genetic complementation assay, we have also gained insights into structure-function relationships in the protein subunit of bacterial RNase P. Specifically, we were able to demonstrate that the bacterial RNase P protein uses one domain to recognize its cognate catalytic RNA subunit and another domain to recognize the 5' leader sequences of its precursor tRNA substrates. The plasticity of the substrate-binding cleft has also been demonstrated by both chemical and genetic rescue experiments. These results, taken together with earlier kinetic studies, have enabled us to understand how the bacterial RNase P protein subunit is able to enhance the rate of chemical cleavage 10-fold and enhance substrate binding 10,000-fold over the RNA alone ptRNA-processing reaction. Finally, we report an interesting study that demonstrates how the Escherichia coli RNase P protein subunit lacking a metal affinity tag can be purified under denaturing conditions using immobilized metal affinity chromatography (IMAC). We are not aware of a precedent in this regard and report these results as a potential new method for the purification of a protein lacking metal affinity tags under denaturing conditions using IMAC.
Author:
Publisher:
ISBN:
Category : Medicine
Languages : en
Pages : 2292
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Book Description
Vols. for 1963- include as pt. 2 of the Jan. issue: Medical subject headings.
Author: Frank J. Schmidt
Publisher: Humana Press
ISBN: 9781493918959
Category : Medical
Languages : en
Pages : 0
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Book Description
In this volume expert researchers in the field detail many of the methods which are now commonly used to study RNA. These methods are presented as a guidebook to scientists who are experienced with RNA research and want to brush up on a new technique. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls. Thorough and intuitive, RNA-RNA Interactions: Methods and Protocols guides scientists investigating biological systems and studying RNA.
Author: Kiyoshi Nagai
Publisher: Oxford University Press, USA
ISBN:
Category : Medical
Languages : en
Pages : 302
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Book Description
The study of RNA-protein interactions is crucial to understanding the mechanisms and control of gene expression and protein synthesis. The realization that RNAs are often far more biologically active than was previously appreciated has stimulated a great deal of new research in this field. Uniquely, in this book, the world's leading researchers have collaborated to produce a comprehensive and current review of RNA-protein interactions for all scientists working in this area. Timely, comprehensive, and authoritative, this new Frontiers title will be invaluable for all researchers in molecular biology, biochemistry and structural biology.
