A Structure/function Analysis of the Interaction of the Escherichia Coli NusA Protein with RNA Polymerase, the Phage Lambda N Protein, and Nut Site RNA. PDF Download
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Languages : en
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Author: Thien-Fah Mah
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Languages : en
Pages : 0
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NusA is an 'E. coli' protein that controls transcription elongation, termination and antitermination. In this thesis, I show that the functions of NusA in transcription are facilitated by interactions with RNA polymerase, RNA and the [lambda] N protein. Use of a series of deletion constructs of NusA allowed me to identify specific regions of NusA involved in specific interactions and in various aspects of NusA function. Genetic evidence suggested that NusA may interact with the 'boxA ' portion of the N-utilization site ('nut' site= ' boxA, interbox,' and 'boxB'). By constructing multiple nucleotide substitutions in the 'nut' site, I showed that the identities of certain nucleotides at the 3' end of ' boxA' and in the 'interbox ' were important for NusA to associate with an N-'nut' site complex. NusA association with RNA in the presence of N is presumably facilitated by its S1 and KH homology regions, two types of RNA-binding domains in NusA. Elimination or mutation of the S1 homology region prevented the association of NusA with an N-' nut' site complex. Using affinity chromatography experiments, I found that RNA polymerase bound equally well to an amino-terminal RNA polymerase-binding region in amino acids 1-137 and a carboxy-terminal RNA polymerase-binding region in amino acids 232-495 of NusA. By contrast, the à subunit of RNA polymerase only bound to the carboxy-terminal RNA polymerase-binding region of NusA. N protein also bound to a carboxy-terminal region of NusA, and both N and à allowed NusA to associate with RNA in a gel mobility shift assay. When the carboxy-terminal region of NusA was deleted in NusA (1-348), the loss of N-binding and Ã-binding ability did not abolish NusA function in termination and antitermination assays. This minimal functional NusA protein retained the KH and S1 homology regions and the amino-terminal RNA polymerase-binding region. Unlike full length NusA (1-495), NusA (1-416) could bind RNA on its own. These observations suggest that the carboxy-terminal region of NusA inhibits RNA binding and that this inhibition can be relieved by interaction with the [lambda] N protein or the à subunit of RNA polymerase.
Author: Ying Zhou
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Category :
Languages : en
Pages : 396
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Author: Richard Calendar
Publisher: Oxford University Press
ISBN: 0195148509
Category : Science
Languages : en
Pages : 761
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This authoritative, timely, and comprehensively referenced compendium on the bacteriophages explores current views of how viruses infect bacteria. In combination with classical phage molecular genetics, new structural, genomic, and single-molecule technologies have rendered an explosion in our knowledge of phages. Bacteriophages, the most abundant and genetically diverse type of organism in the biosphere, were discovered at the beginning of the 20th century and enjoyed decades of used as anti-bacterial agents before being eclipsed by the antibiotic era. Since 1988, phages have come back into the spotlight as major factors in pathogenesis, bacterial evolution, and ecology. This book reveals their compelling elegence of function and their almost inconceivable diversity.Much of the founding work in molecular biology and structural biology was done on bacteriophages. These are widely used in molecular biology research and in biotechnology, as probes and markers, and in the popular method of assesing gene expression.
Author: K.H. Nierhaus
Publisher: Springer Science & Business Media
ISBN: 1461524075
Category : Science
Languages : en
Pages : 741
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Proceedings of an international conference held in Berlin, Germany, October 31-November 5, 1992
Author: Laura Magdolna Heisler
Publisher:
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Category :
Languages : en
Pages : 496
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Publisher: Walter de Gruyter GmbH & Co KG
ISBN: 3110476622
Category : Science
Languages : en
Pages : 172
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Zeitschrift für Kristallographie. Supplement Volume 36 presents the complete Abstracts of all contributions to the 24th Annual Conference of the German Crystallographic Society in Stuttgart (Germany) 2016: - Plenary Talks - Microsymposia - Poster Session Supplement Series of Zeitschrift für Kristallographie publishes Abstracts of international conferences on the interdisciplinary field of crystallography.
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Category : Dissertations, Academic
Languages : en
Pages : 896
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Category : Medicine
Languages : en
Pages : 1052
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Category : Dissertation abstracts
Languages : en
Pages : 848
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