Structural dynamics of intrinsically disordered proteins

Language: English

Published by LAP LAMBERT Academic Publishing Jan 2013, 2013

3659326062 / 9783659326066

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This item is printed on demand - Print on Demand Titel. Neuware -The homodimeric umuD gene products play key roles in regulating the cellular response to DNA damage in Escherichia coli. UmuD2 is composed of 139-amino acid subunits and is upregulated as part of the SOS DNA damage response. Subsequently, damage-induced RecA:ssDNA nucleoprotein filaments mediate the slow autocleavage of the N-terminal 24-amino acid arms of UmuD2 yielding UmuD¿2. It was previously proposed that UmuD cleaves only in the trans conformation, in which the arm of one monomer utilizes that active site of the adjacent monomer for cleavage. Cleavage in trans would therefore require dimerization. However, isoenergetic models of UmuD2 suggested that the arms may adopt cis (intramolecular) or trans (intermolecular) conformations, and may be unbound from or bound to the globular C-terminal domain. The dynamic nature of the N-terminal arms may explain how a number of distinct protein-protein contacts that prevent and facilitate mutagenic translesion synthesis (TLS) are made. Here we discuss how the conformation and dynamics of the UmuD proteins regulate the DNA damage response.OmniScriptum SRL, Str. Armeneasca 28/1, office 1, 2012 Chisinau 168 pp. Englisch.

Seller Inventory # 9783659326066

Title
Structural dynamics of intrinsically disordered proteins
Author
Jaylene Ollivierre
Publisher
LAP LAMBERT Academic Publishing Jan 2013
Publication year
2013
Condition
Neu
Binding
Taschenbuch
Language
English
ISBN 10
3659326062
ISBN 13
9783659326066
Item weight
268 grams
Dimensions
220x150x11 mm

buchversandmimpf2000

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