H-NS is a part of a thermally controlled mechanism for bacterial gene regulation
نویسندگان
چکیده
منابع مشابه
Nucleoprotein filament formation is the structural basis for bacterial protein H-NS gene silencing
H-NS is an abundant nucleoid-associated protein in bacteria that globally silences genes, including horizontally-acquired genes related to pathogenesis. Although it has been shown that H-NS has multiple modes of DNA-binding, which mode is employed in gene silencing is still unclear. Here, we report that in H-NS mutants that are unable to silence genes, are unable to form a rigid H-NS nucleoprot...
متن کاملA model of H-NS mediated compaction of bacterial DNA.
The histone-like nucleoid structuring protein (H-NS) is a nucleoid-associated protein, which is involved in both gene regulation and DNA compaction. H-NS can bind to DNA in two different ways: in trans, by binding to two separate DNA duplexes, or in cis, by binding to different sites on the same duplex. Based on scanning force microscopy imaging and optical trap-driven unzipping assays, it has ...
متن کاملH-NS-Dependent regulation of flagellar synthesis is mediated by a LysR family protein.
H-NS regulates the flagellar master operon (flhDC) and thus is necessary for flagellation of Escherichia coli. However, the molecular mechanism of its regulation has remained unknown. Genetic screening of a transposon insertion abolishing the H-NS effect revealed a previously unidentified gene, named hdfR, encoding a LysR family protein. Binding of purified HdfR to the flhDC promoter was demons...
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deployable scissor type structures are composed of the so-called scissor-like elements (sles), which are connected to each other at an intermediate point through a pivotal connection and allow them to be folded into a compact bundle for storage or transport. several sles are connected to each other in order to form units with regular polygonal plan views. the sides and radii of the polygons are...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2005
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20050453