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Rho factor information


Transcription termination factor Rho
Rho factor homohexamer
Identifiers
OrganismE. coli
Symbolrho
UniProtP0AG30
Search for
StructuresSwiss-model
DomainsInterPro

A ρ factor (Rho factor) is a bacterial protein involved in the termination of transcription.[1] Rho factor binds to the transcription terminator pause site, an exposed region of single stranded RNA (a stretch of 72 nucleotides) after the open reading frame at C-rich/G-poor sequences that lack obvious secondary structure.[2]

Rho factor is an essential transcription protein in bacteria.[3] In Escherichia coli, it is a ~274.6 kD hexamer of identical subunits. Each subunit has an RNA-binding domain and an ATP-hydrolysis domain. Rho is a member of the RecA/SF5 family of ATP-dependent hexameric helicases that function by wrapping nucleic acids around a single cleft extending around the entire hexamer. Rho functions as an ancillary factor for RNA polymerase.

There are two types of transcriptional termination in bacteria, rho-dependent termination and intrinsic termination (also called Rho-independent termination). Rho-dependent terminators account for about half of the E. coli factor-dependent terminators. Other termination factors discovered in E. coli include Tau and nusA. Rho-dependent terminators were first discovered in bacteriophage genomes.

  1. ^ Said N, Hilal T, Sunday ND, Khatri A, Bürger J, Mielke T, et al. (January 2021). "Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ". Science. 371 (6524). doi:10.1126/science.abd1673. hdl:21.11116/0000-0007-AD1D-7. PMC 7864586. PMID 33243850.
    • Emily Caldwell (November 26, 2020). "Study revealing the secret behind a key cellular process refutes biology textbooks". Phys.org.
  2. ^ Slonczewski J, Foster JW (2009). Microbiology: An Evolving Science. New York: W.W. Norton &, Incorporated. ISBN 978-0-393-11332-7.
  3. ^ Pradeepkiran JA, Kumar KK, Kumar YN, Bhaskar M (2015). "Modeling, molecular dynamics, and docking assessment of transcription factor rho: a potential drug target in Brucella melitensis 16M". Drug Design, Development and Therapy. 9: 1897–912. doi:10.2147/DDDT.S77020. PMC 4386771. PMID 25848225.

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shows significant similarity to hexameric DNA helicases (especially the Rho factor), and the entire enzyme region shows some similarity to H+ -powered T3SS...

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