Structural and Mechanistic Differences Between a Protein and an RNA-containing RNase P PDF Download
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Author: Brian Charles Thomas
Publisher:
ISBN:
Category :
Languages : en
Pages : 284
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Author: Brian Charles Thomas
Publisher:
ISBN:
Category :
Languages : en
Pages : 284
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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: Jing Zhao
Publisher:
ISBN:
Category : Molecular recognition
Languages : en
Pages : 165
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Book Description
The affinity and kinetics of RNA and protein association depends on the stability of the RNA-protein complex as well as the structure and stability of the free RNA and protein. While much is known about how proteins and enzymes bind their specific sites in RNA, less is understood about the effects of RNA sequence and structure contexts surrounding these specific binding sites on binding. Ribonuclease P (RNase P) is a ribonucleoprotein enzyme involved in tRNA processing that relies on the protein subunit that forms essential contacts to a linear sequence of 3-8 nucleotides in the 5′ leader of precursor tRNA (ptRNA). Therefore, binding is likely to be influenced by the presence of competing secondary structure in the free RNA leader sequence. To address this issue, we pursued two primary lines of investigation. First, we compared the kinetics of RNA cleavage in monocistronic and polycistronic ptRNAs, which offers the opportunity to investigate the role of local RNA contexts on recognition. Kinetic analysis by using single turnover kinetics in vitro, cleavage site mapping and uniform substrate labelling on polycistronic ptRNAval VW reproduces the 3′ to 5′ ordered processing observed in vivo suggesting this is the most predominant pathway by RNase P. In-line probing further reveals the effects of both ptRNAs order and leader structure on directional processing. Kinetic analysis on valV and valW individually suggests that valV is an intrinsically slow and valW is an intrinsically fast substrate due to the leader structure on valV. Therefore, ordered processing can arise from the ability of genomically encoded sequences to form inhibitory secondary structure proximal to the RNase P cleavage site that inhibits processing. In a parallel experiment, we designed three different ptRNA substrate pools with randomized leader sequences proximal to the RNase P cleavage site, but with different RNA sequences appended upstream. Using a high throughput approach the rate constants for all the individual RNA substrates in the population were determined, and the resulting data was analyzed to test the effect of variation in both sequence and secondary structure on processing specificity globally. The effects of two upstream extensions (21A and 21B) containing transversion mutations were compared. Also, a third population (21C) was designed to form a stable stem loop that should insulate the randomized protein binding site from the effects of inhibitory interactions with additional leader sequences. Using a high-throughput sequencing kinetics (HiTS-KIN) method, we determined the rate constants for all sequence variants at N (-1) to N(-6) in the 21A, B and C backgrounds. Comparison of the three HiTS-KIN data clearly demonstrates that formation of inhibitory secondary structures influences the association kinetics of a subset of substrates. Together, the comparative HiTS-KIN analyses in vitro and mechanistic basis of ordered genomic encoded polycistronic ptRNAs processing demonstrate the contribution of structure and sequence variations to RNase P processing specificity. Surprisingly, the results from both studies reveal several substrates that are processed rapidly despite the presence of structure in the 5′ leader sequence. Altogether, these results provide a better understanding of intrinsic molecular recognition properties of similar multiple substrate RNA processing enzymes, reveal in detail the effects of sequence and structure contexts on RNA molecular recognition, and suggest new questions for future study of this important area of research.
Author: Fenyong Liu
Publisher: Springer
ISBN: 9781441911438
Category : Science
Languages : en
Pages : 283
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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:
Publisher:
ISBN:
Category :
Languages : en
Pages :
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RNase P catalyzes tRNA 5'-end maturation in all organisms and organelles. The enzyme is composed of a single RNA subunit plus a number of proteins that increases from bacteria (one protein) over archaea (at least four proteins) to eukarya (nine to ten proteins). Conserved base identities indicate that the RNase P RNA subunits (P RNAs) from all three kingsdoms of life stem from a common ancestor. Yet, only in bacteria the P RNA alone is substantially active in vitro without the protein, whereas archaeal and eukaryal P RNAs are more dependent on the contribution of their protein moieties and display only residual activity when these are absent. RNase P thus represents a natural model system for the switch from ribozyme to ribonucleoprotein enzyme, generally accepted to have occurred during natural evolution of the RNA world to the protein world. The RNA subunit of cyanelle RNase P from Cyanophora paradoxa contains essentially all structural elements of bacterial P RNAs, but has been reported to be catalytically inactive. In contrast to these previous observations, we were able to detect activity of this P RNA in the absence of protein cofactors. Furthermore, the C. paradoxa P RNA forms a functional holoenzyme with proteobacterial P proteins. Analysis of C- and S-domain swaps between cyanelle and Escherichia coli P RNA revealed that their domains have the capacity to cooperate, because the hybrid RNAs were functional. However, activities of the chimeras lagged behind the catalytic performance of the bacterial P RNA, suggesting that both the C- and S-domain of the cyanelle P RNA are weakly functional, thus limiting the activity of each type of chimera (EC or CE). In addition or alternatively, domain interaction and overall folding may be suboptimal in the chimeras, as it likely is in the wild-type cyanelle P RNA. Furthermore, the organellar ribozyme is unusual compared to the consensus of bacterial P RNAs: RNA-alone activity is low and structural alterations as small as.
Author: Pierre Pontarotti
Publisher: Springer Nature
ISBN: 3030572463
Category : Science
Languages : en
Pages : 389
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Book Description
This book includes 16 selected contributions presented at the 23rd Evolutionary Biology Meeting, which took place in Marseille in September 2019. The annual Evolutionary Biology Meetings in Marseille serve to gather leading evolutionary biologists and other scientists using evolutionary biology concepts, e.g. for medical research. The aim of these meetings is to promote the exchange of ideas to encourage interdisciplinary collaborations. Offering an up-to-date overview of recent findings in the field of evolutionary biology, this book is an invaluable source of information for scientists, teachers and advanced students.
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages :
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Author: Torben Heick Jensen
Publisher: Springer Science & Business Media
ISBN: 1441978410
Category : Medical
Languages : en
Pages : 161
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Book Description
The diversity of RNAs inside living cells is amazing. We have known of the more “classic” RNA species: mRNA, tRNA, rRNA, snRNA and snoRNA for some time now, but in a steady stream new types of molecules are being described as it is becoming clear that most of the genomic information of cells ends up in RNA. To deal with the enormous load of resulting RNA processing and degradation reactions, cells need adequate and efficient molecular machines. The RNA exosome is arising as a major facilitator to this effect. Structural and functional data gathered over the last decade have illustrated the biochemical importance of this multimeric complex and its many co-factors, revealing its enormous regulatory power. By gathering some of the most prominent researchers in the exosome field, it is the aim of this volume to introduce this fascinating protein complex as well as to give a timely and rich account of its many functions. The exosome was discovered more than a decade ago by Phil Mitchell and David Tollervey by its ability to trim the 3’end of yeast, S. cerevisiae, 5. 8S rRNA. In a historic account they laid out the events surrounding this identification and the subsequent birth of the research field. In the chapter by Kurt Januszyk and Christopher Lima the structural organization of eukaryotic exosomes and their evolutionary counterparts in bacteria and archaea are discussed in large part through presentation of structures.
Author:
Publisher: Elsevier
ISBN: 0080522572
Category : Science
Languages : en
Pages : 555
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Book Description
This second volume on ribonucleases provides up-to-date, methods-related information on these enzymes. Of particular interest to researchers will be the discussion of artificial and engineered ribonucleases, as well as the application of ribonucleases in medicine and biotechnology.The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.
Author:
Publisher: Academic Press
ISBN: 0128118776
Category : Science
Languages : en
Pages : 277
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Book Description
Structural and Mechanistic Enzymology, Volume 109, the latest release in the Advances in Protein Chemistry and Structural Biology series, is an essential resource for protein chemists. Chapters in this new volume include Collagenolytic Matrix Metalloproteinase Structure–Function Relationships: Insights from Molecular Dynamics Studies, Computational Glycobiology: Mechanistic Studies of Carbohydrate-Active Enzymes and Implication for Inhibitor Design, Computational Biochemistry-Enzyme Mechanisms Explored, and A Paradigm for C-H Bond Cleavage: Structural and Functional Aspects of Transition State Stabilization by Mandelate Racemase. This series presents new information on protocols and analysis of proteins, with each volume guest edited by leading experts in a broad range of protein-related topics. This volume presents state-of-the-art contributions, providing insights into the relationship between enzyme structure, catalysis, and function. - Provides cutting-edge developments in protein chemistry and structural biology - Features new information about protocols and analysis of proteins - Contains chapters written by authorities in their respective fields - Targeted to a wide audience of researchers, specialists and students
