Keeping up to speed with the transcription termination factor Rho motor
نویسندگان
چکیده
منابع مشابه
Rho Factor: Transcription Termination in Four Steps
Rho factor is a hexameric ring-shaped helicase which terminates transcription in Escherichia coli. Two recent crystal structures of Rho in complex with nucleic acid reveal how this helicase ring loads onto mRNA and encircles it.
متن کاملMechanochemistry of transcription termination factor Rho.
Rho is a ring-shaped hexameric motor protein that translocates along nascent mRNA transcript and terminates transcription of select genes in bacteria. Using a numerical optimization algorithm that simultaneously fits all of the presteady-state ATPase kinetic data, we determine how Rho utilizes the chemical energy of ATP hydrolysis to translocate RNA. A random hydrolysis mechanism is ruled out b...
متن کاملATP-dependent motor activity of the transcription termination factor Rho from Mycobacterium tuberculosis
The bacterial transcription termination factor Rho-a ring-shaped molecular motor displaying directional, ATP-dependent RNA helicase/translocase activity-is an interesting therapeutic target. Recently, Rho from Mycobacterium tuberculosis (MtbRho) has been proposed to operate by a mechanism uncoupled from molecular motor action, suggesting that the manner used by Rho to dissociate transcriptional...
متن کاملTranscription termination factor Rho is essential for Micrococcus luteus.
The growth of Micrococcus luteus, a soil microorganism that belongs to the high-G+C gram-positive phylogenetic group, is prevented by bicyclomycin, an antibiotic that inhibits the activity of the M. luteus transcription termination factor Rho. A mutant that can grow in 0.3 mM bicyclomycin has a Rho that is insensitive to bicyclomycin and has the single amino acid residue change of Asp474 to Gly...
متن کاملATPase activity of transcription-termination factor rho: functional dimer model.
Transcription-termination factor rho of Escherichia coli functions as an RNA-dependent ATPase that causes transcript release at specific rho-dependent termination sites on the DNA template. Rho exists as a hexagon of identical subunits, physically organized as a trimer of dimers with D3 symmetry. The structural asymmetry of the dimer is reflected in the binding properties of rho; each dimer has...
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ژورنال
عنوان ژورنال: Transcription
سال: 2010
ISSN: 2154-1264,2154-1272
DOI: 10.4161/trns.1.2.12232