NDLI: Uncoupling of the DNA topoisomerase and replication activities of an initiator protein.

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Synthesis of the early light-inducible protein is controlled by blue light and related to light stress.

Multiple occurrences of mutualism in the yucca moth lineage.

Sequence and expression in Escherichia coli of the 40-kDa subunit of activator 1 (replication factor C) of HeLa cells.

High frequency of single-base transitions and extreme frequency of precise multiple-base reversion mutations in poliovirus.

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Expression cloning of a common receptor for parathyroid hormone and parathyroid hormone-related peptide from rat osteoblast-like cells: a single receptor stimulates intracellular accumulation of both cAMP and inositol trisphosphates and increases intracellular free calcium.

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Uncoupling of the DNA topoisomerase and replication activities of an initiator protein.

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Uncoupling of the DNA topoisomerase and replication activities of an initiator protein.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Khan, S. A. Dempsey, L. A. Birch, P.
Description	Author Affiliation: Dempsey LA ( Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, PA 15261.);
Abstract	The replication initiator proteins encoded by the pT181 and related plasmids have sequence-specific DNA binding and topoisomerase activities. These proteins create a site-specific nick in one strand of the DNA at the origin of replication that serves as a primer for the initiation of replication. To define the regions of the pT181-encoded initiator protein, RepC, that are involved in its DNA binding, topoisomerase, and replication activities, we have carried out site-directed mutagenesis of the repC gene. Analysis of mutant RepC proteins in vitro and in vivo has identified the amino acids that are critical for its various biochemical activities. The DNA binding domain of RepC was found to be located near its C-terminal region and was different from the domain involved in its sequence-specific topoisomerase activity. These studies also showed that the DNA topoisomerase activity of the initiator protein can be uncoupled from its tight noncovalent DNA binding and replication activities.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Genetics DNA Replication Plasmids Chemistry Binding Sites DNA Topoisomerases, Type I Metabolism DNA-Binding Proteins Genetic Complementation Test Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Recombinant Proteins Staphylococcus Aureus Structure-Activity Relationship Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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