Title |
Rho-dependent Transcription Termination: More Questions than Answers |
Author |
Sharmistha Banerjee, Jisha Chalissery, Irfan Bandey, and Ranjan Sen* |
Address |
Laboratory of Transcription Biology, Center for DNA Fingerprinting and Diagnostics, ECIL Road,Nacharam, Hyderabad-500076, India. |
Bibliography |
Journal of Microbiology, 44(1),11-22, 2006,
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DOI |
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Key Words |
Escherichia coli protein Rho is required for the factor-dependent transcription termination by an helicase |
Abstract |
Escherichia coli protein Rho is required for the factor-dependent transcription termination by an
RNA polymerase and is essential for the viability of the cell. It is a homohexameric protein that
recognizes and binds preferably to C-rich sites in the transcribed RNA. Once bound to RNA, it
utilizes RNA-dependent ATPase activity and subsequently ATPase-dependent helicase activity to
unwind RNA-DNA hybrids and release RNA from a transcribing elongation complex. Studies
over the past few decades have highlighted Rho as a molecule and have revealed much of its
mechanistic properties. The recently solved crystal structure could explain many of its physiological
functions in terms of its structure. Despite all these efforts, many of the fundamental questions
pertaining to Rho recognition sites, differential ATPase activity in response to different
RNAs, translocation of Rho along the nascent transcript, interactions with elongation complex and
finally unwinding and release of RNA remain obscure. In the present review we have attempted
to summarize ‘the knowns’ and ‘the unknowns’ of the Rho protein revealed by the recent developments
in this field. An attempt has also been made to understand the physiology of Rho in the
light of its phylogeny. |
Download PDF |
03 JM2005-161.pdf |