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Molecular modeling of RecX reveals its mode of interaction with RecA.
Biochem Biophys Res Commun. 2003 Dec 19; 312(3):615-22.BB

Abstract

The protein RecA is involved in homologous recombination, DNA repair and also catalyzes DNA strand exchange. RecX gene is downstream of recA and the gene product RecX is supposed to be important for RecA regulation. Recombinant RecX is purified to homogeneity, and circular dichroism (CD) and FTIR spectroscopy show the protein to exist mostly in helical conformation. The fluorescence emission maxima of the native and the denatured protein and the steady-state fluorescence quenching studies with acrylamide indicate the presence of tryptophan residues partially exposed to the bulk solvent. Denaturation studies with urea and guanidine hydrochloride by use of spectroscopic methods, fluorescence, and CD also confirm the instability of the protein and unfolding occurs following a two-state model. Mass spectrometry and gel permeation chromatography suggest the monomeric form of the protein. Molecular modeling of RecX represents the molecule as extended and helical bundle in conformity with the spectroscopic results. To understand the mechanism of RecX in the regulation of RecA the structural model of RecA-RecX has been discussed. In this proposed model, entry of RecX into hexameric RecA filament prevents binding of ssDNA and also inhibits ATPase activity.

Authors+Show Affiliations

Department of Biotechnology, Indian Institute of Technology, Kharagpur 721302, India.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

14680809

Citation

Mishra, Subhra, et al. "Molecular Modeling of RecX Reveals Its Mode of Interaction With RecA." Biochemical and Biophysical Research Communications, vol. 312, no. 3, 2003, pp. 615-22.
Mishra S, Mazumdar PA, Dey J, et al. Molecular modeling of RecX reveals its mode of interaction with RecA. Biochem Biophys Res Commun. 2003;312(3):615-22.
Mishra, S., Mazumdar, P. A., Dey, J., & Das, A. K. (2003). Molecular modeling of RecX reveals its mode of interaction with RecA. Biochemical and Biophysical Research Communications, 312(3), 615-22.
Mishra S, et al. Molecular Modeling of RecX Reveals Its Mode of Interaction With RecA. Biochem Biophys Res Commun. 2003 Dec 19;312(3):615-22. PubMed PMID: 14680809.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular modeling of RecX reveals its mode of interaction with RecA. AU - Mishra,Subhra, AU - Mazumdar,Pooja Anjali, AU - Dey,Joykrishna, AU - Das,Amit Kumar, PY - 2003/10/15/received PY - 2003/12/19/pubmed PY - 2004/3/16/medline PY - 2003/12/19/entrez SP - 615 EP - 22 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 312 IS - 3 N2 - The protein RecA is involved in homologous recombination, DNA repair and also catalyzes DNA strand exchange. RecX gene is downstream of recA and the gene product RecX is supposed to be important for RecA regulation. Recombinant RecX is purified to homogeneity, and circular dichroism (CD) and FTIR spectroscopy show the protein to exist mostly in helical conformation. The fluorescence emission maxima of the native and the denatured protein and the steady-state fluorescence quenching studies with acrylamide indicate the presence of tryptophan residues partially exposed to the bulk solvent. Denaturation studies with urea and guanidine hydrochloride by use of spectroscopic methods, fluorescence, and CD also confirm the instability of the protein and unfolding occurs following a two-state model. Mass spectrometry and gel permeation chromatography suggest the monomeric form of the protein. Molecular modeling of RecX represents the molecule as extended and helical bundle in conformity with the spectroscopic results. To understand the mechanism of RecX in the regulation of RecA the structural model of RecA-RecX has been discussed. In this proposed model, entry of RecX into hexameric RecA filament prevents binding of ssDNA and also inhibits ATPase activity. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/14680809/Molecular_modeling_of_RecX_reveals_its_mode_of_interaction_with_RecA_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006291X03022150 DB - PRIME DP - Unbound Medicine ER -