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Vibrio cholerae YaeO is a Structural Homologue of RNA Chaperone Hfq that Inhibits Rho-dependent Transcription Termination by Dissociating its Hexameric State.
J Mol Biol 2019JM

Abstract

Rho-dependent transcription termination is a well-conserved process in bacteria. The Psu and YaeO proteins are the two established inhibitors of the ATP-dependent RNA helicase Rho protein of Escherichia coli. Here, we show a detailed sequence and phylogenetic analysis demonstrating that Vibrio cholerae YaeO (VcYaeO) is significantly distinct from its E. coli counterpart. VcYaeO induces significant growth defect on in vivo expression and inhibits in vitro functions of the V. cholerae Rho on directly binding to the latter. Through various biophysical techniques, we showed that interaction of VcYaeO disrupts the oligomeric state of the VcRho. Structure of VcYaeO solved at 1.75 Å resolution, the first crystal structure of a YaeO protein, demonstrates a beta-sandwich fold distinct from the NMR structure of the EcYaeO. Interestingly, VcYaeO structurally resembles the Hfq protein, and like the latter, it exhibits ssDNA/RNA-binding properties. Docking studies demonstrate probable interactions of VcYaeO with VcRho and mode of inhibition of RNA binding to Rho. We propose that VcYaeO inhibits the function of the Rho protein via disruption of the latter's hexameric assembly and also likely by sequestering the RNA from the Rho primarybinding sites.

Authors+Show Affiliations

Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, HBNI, 1/AF Bidhan Nagar, Kolkata 700064, India.Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, HBNI, 1/AF Bidhan Nagar, Kolkata 700064, India.Laboratory of Transcription, Center for DNA Fingerprinting and Diagnostics, Tuljaguda Complex, 4-1-714 Mouzamjahi Road, Nampally, Hyderabad 500 001, India.High Pressure & Synchrotron Radiation Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400085, India.Laboratory of Transcription, Center for DNA Fingerprinting and Diagnostics, Tuljaguda Complex, 4-1-714 Mouzamjahi Road, Nampally, Hyderabad 500 001, India.Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, HBNI, 1/AF Bidhan Nagar, Kolkata 700064, India. Electronic address: udayaditya.sen@saha.ac.in.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31628950

Citation

Pal, Kamalendu, et al. "Vibrio Cholerae YaeO Is a Structural Homologue of RNA Chaperone Hfq That Inhibits Rho-dependent Transcription Termination By Dissociating Its Hexameric State." Journal of Molecular Biology, 2019.
Pal K, Yadav M, Jain S, et al. Vibrio cholerae YaeO is a Structural Homologue of RNA Chaperone Hfq that Inhibits Rho-dependent Transcription Termination by Dissociating its Hexameric State. J Mol Biol. 2019.
Pal, K., Yadav, M., Jain, S., Ghosh, B., Sen, R., & Sen, U. (2019). Vibrio cholerae YaeO is a Structural Homologue of RNA Chaperone Hfq that Inhibits Rho-dependent Transcription Termination by Dissociating its Hexameric State. Journal of Molecular Biology, doi:10.1016/j.jmb.2019.09.019.
Pal K, et al. Vibrio Cholerae YaeO Is a Structural Homologue of RNA Chaperone Hfq That Inhibits Rho-dependent Transcription Termination By Dissociating Its Hexameric State. J Mol Biol. 2019 Oct 16; PubMed PMID: 31628950.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Vibrio cholerae YaeO is a Structural Homologue of RNA Chaperone Hfq that Inhibits Rho-dependent Transcription Termination by Dissociating its Hexameric State. AU - Pal,Kamalendu, AU - Yadav,Malti, AU - Jain,Sriyans, AU - Ghosh,Biplab, AU - Sen,Ranjan, AU - Sen,Udayaditya, Y1 - 2019/10/16/ PY - 2019/07/11/received PY - 2019/09/25/revised PY - 2019/09/26/accepted PY - 2019/10/20/pubmed PY - 2019/10/20/medline PY - 2019/10/20/entrez KW - ATPase KW - Antitermination KW - Cell viability KW - Fluorescence quenching KW - X-ray crystallography JF - Journal of molecular biology JO - J. Mol. Biol. N2 - Rho-dependent transcription termination is a well-conserved process in bacteria. The Psu and YaeO proteins are the two established inhibitors of the ATP-dependent RNA helicase Rho protein of Escherichia coli. Here, we show a detailed sequence and phylogenetic analysis demonstrating that Vibrio cholerae YaeO (VcYaeO) is significantly distinct from its E. coli counterpart. VcYaeO induces significant growth defect on in vivo expression and inhibits in vitro functions of the V. cholerae Rho on directly binding to the latter. Through various biophysical techniques, we showed that interaction of VcYaeO disrupts the oligomeric state of the VcRho. Structure of VcYaeO solved at 1.75 Å resolution, the first crystal structure of a YaeO protein, demonstrates a beta-sandwich fold distinct from the NMR structure of the EcYaeO. Interestingly, VcYaeO structurally resembles the Hfq protein, and like the latter, it exhibits ssDNA/RNA-binding properties. Docking studies demonstrate probable interactions of VcYaeO with VcRho and mode of inhibition of RNA binding to Rho. We propose that VcYaeO inhibits the function of the Rho protein via disruption of the latter's hexameric assembly and also likely by sequestering the RNA from the Rho primarybinding sites. SN - 1089-8638 UR - https://www.unboundmedicine.com/medline/citation/31628950/Vibrio_cholerae_YaeO_is_a_structural_homologue_of_RNA_chaperone_Hfq_that_inhibits_Rho-dependent_transcription_termination_by_dissociating_its_hexameric_state L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(19)30574-1 DB - PRIME DP - Unbound Medicine ER -