INTEGRATION HOST FACTOR - A PROTEIN FOR ALL REASONS
INTEGRATION HOST FACTOR - A PROTEIN FOR ALL REASONS
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DOI:
10.1016/0092-8674(88)90213-9
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发表时间:
1988-11-18
期刊:
影响因子:
64.5
通讯作者:
FRIEDMAN, DI
中科院分区:
文献类型:
--
作者:
FRIEDMAN, DI
The identification and characterization of the Escherichia coli DNA binding protein integration host factor (IHF) is an elegant example of how a well-characterized virus can be employed in the analysis of a host function. In this case, Nash and coworkers, through their landmark in vitro studies of coliphage h site-specific recombination (reiewed in Nash, 1981), have identified a protein that plays roles not only in other recombination reactions, but also in DNA replication and regulation of gene expression. IHF belongs to a class of structurally related “histonelike” proteins that can wrap DNA into higher-order structures (Drlica and Rouviere-Yaniv, 1987). The most abundant of these proteins in E. coli is HU, and others have been found in a number of bacterial genera as well as archaebacteria.In addition to site-specific recombination, other aspects of h development influenced by IHF have been fertile sources of information about this protein. I will initially focus on studies with h that serve to present the basic information about IHF and then examine the various roles for IHF derived from studies of E. coli and some of its other phages and plasmids.