NMR Structural Studies of the RNA-binding Domain of Rho Protein PDF Download
Are you looking for read ebook online? Search for your book and save it on your Kindle device, PC, phones or tablets. Download NMR Structural Studies of the RNA-binding Domain of Rho Protein PDF full book. Access full book title NMR Structural Studies of the RNA-binding Domain of Rho Protein by Deborah Marilyn Briercheck. Download full books in PDF and EPUB format.
Author: Deborah Marilyn Briercheck
Publisher:
ISBN:
Category :
Languages : en
Pages : 538
Get Book Here
Book Description
Author: Deborah Marilyn Briercheck
Publisher:
ISBN:
Category :
Languages : en
Pages : 538
Get Book Here
Book Description
Author: Peter W. A. Howe
Publisher:
ISBN:
Category :
Languages : en
Pages :
Get Book Here
Book Description
Author: Zdravko Lorkovic
Publisher: CRC Press
ISBN: 149871336X
Category : Science
Languages : en
Pages : 174
Get Book Here
Book Description
Gene expression in eukaryotes is regulated at different levels, which need to be coordinated to implement the information in the genome. Now it is clear that post-transcriptional regulation of gene expression such as pre-mRNA splicing, mRNA transport, editing, turnover and translation are as important as the control of transcription. In all aspects
Author: David E. Modrak
Publisher:
ISBN:
Category :
Languages : en
Pages : 372
Get Book Here
Book Description
Author: G. R. Hill
Publisher:
ISBN:
Category :
Languages : en
Pages :
Get Book Here
Book Description
Author: Helena Berglund
Publisher:
ISBN: 9789171701510
Category :
Languages : en
Pages : 30
Get Book Here
Book Description
Author:
Publisher: Academic Press
ISBN: 0128019360
Category : Science
Languages : en
Pages : 675
Get Book Here
Book Description
This new volume of Methods in Enzymology continues the legacy of this premier serial with quality chapters authored by leaders in the field. This volume covers research methods in RNA folding and dynamics, RNA-protein interactions and large RNPs. Continues the legacy of this premier serial with quality chapters on structures of large RNA molecules and their complexes
Author: Kiyoshi Nagai
Publisher: Oxford University Press, USA
ISBN:
Category : Medical
Languages : en
Pages : 302
Get Book Here
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.
Author: Sheng Liu
Publisher:
ISBN:
Category :
Languages : en
Pages : 137
Get Book Here
Book Description
Human lysyl aminoacyl tRNA synthetase (hLysRS) is a multi-functional aminoacyl tRNA synthetase which is primarily involved in protein biosynthesis as well as crucial processes ranging from proinflammatory response to signal transduction. One important, non-canonical function of hLysRS is to target lysyl tRNA isoacceptor 3, the HIV-1 reverse transcription primer molecule, for uptake and packaging into new HIV-1 particles. Since the anticodon binding (ACB) domain of hLysRS is required for proper recognition of its cognate tRNA, NMR studies of the ACB domain were conducted to enhance our understanding of how hLysRS interacts with these RNAs during protein biosynthesis as well as HIV-1 viral packaging. The backbone and side chain NMR resonance assignments were obtained for the uniformly 15N-, 13C-labeled ACB domain of hLysRS. With NMR resonance assignments in hand, we mapped the ACB protein surface that is affected by RNA binding via NMR chemical shift perturbation techniques. The RNA molecules studied this way include the anticodon stem-loop of lysyl tRNA isoacceptor 3 (ACSL) and a tRNA-like element (TLE) derived from a region 5' to the primer binding site of the HIV-1 RNA genome (wild type TLE, or wtTLE). The TLE was recently proposed to compete against lysyl tRNA isoacceptor 3 for interaction with the hLysRS which is important for proper primer binding and reverse transcription during the HIV-1 life cycle. Considerable overlap was observed in terms of the ACB surface affected by RNA binding for the ACSL and wtTLE RNAs, which means the ACB domain interacts with the ACSL and wtTLE in a similar manner. This result supports the hypothesis that the TLE can mimic the tRNA anticodon loop in terms of interacting with the ACB domain of hLysRS. An important characteristic of higher eukaryotic forms of lysyl aminoacyl tRNA synthetase (LysRS) is the appendage of an N-terminal domain to the highly conserved ACB and catalytic domains. The function of this N-terminal domain has been proposed to enhance the overall RNA binding affinity which may contribute to the HIV-1 reverse transcription primer uptake and possibly modulate LysRS binding to other proteins; however, its structure still remains unknown. To better elucidate the RNA binding behavior and potential structure of this appendage domain, the backbone and side chain NMR resonance assignments have been achieved for uniformly 15N-, 13C-labeled hLysRS N-terminal domain alone, as well as complexed to ACSL RNA. Based upon the assigned NMR resonances of this protein, the isolated N-terminal domain is mostly unstructured in solution. However, this domain was found to adopt a 27 residue long helical structure only after binding to ACSL RNA. NMR titration studies using different forms of the N-terminal domain protein via segmental labeling reveal that RNA binding by this N-terminal domain is cooperative with the adjacent ACB domain. The fact that the N-terminal domain is unaffected by titration with oligo U or oligo C RNAs regardless of whether the ACB domain is attached suggests that the N-terminal domain may have a preference for structured, possibly stem-loop RNA molecules.
Author: Jenny Cromsigt
Publisher:
ISBN: 9789173050692
Category :
Languages : en
Pages : 51
Get Book Here
Book Description
