NDLI: Characterization of the RstB2 protein, the DNA-binding protein of CTXϕ phage from Vibrio cholerae

Content Provider	Springer Nature Link
Author	Falero, Alina Marrero, Karen Trigueros, Sonia Fando, Rafael
Copyright Year	2014
Abstract	The low abundant protein RstB2, encoded in the RS2 region of CTXϕ, is essential for prophage formation. However, the only biochemical activity so far described is the single/double-stranded DNA-binding capacity of that protein. In this paper, a recombinant RstB2 (rRstB2) protein was overexpressed in E. coli with a yield of 58.4 mg l$^{−1}$ in shaken cultures, LB broth. The protein, purified to homogeneity, showed an identity with rRstB2 by peptide mass fingerprinting. The apparent molecular weight of the RstB2 native protein suggests that occurs mostly as a monomer in solution. The monomers were able of reacting immediately upon exposure to DNA molecules. After a year of storage at −20 °C, the protein remains biologically active. Bioinformatics analysis of the amino acid sequence of RstB2 predicts the C-end of this protein to be disordered and highly flexible, like in many other single-stranded DNA-binding proteins. When compared with the gVp of M13, conserved amino acids are found at structurally or functionally important relative positions. These results pave the way for additional studies of structure and molecular function of RstB2 for the biology of CTXϕ.
Starting Page	518
Ending Page	527
Page Count	10
File Format	PDF
ISSN	09208569
Journal	Virus Genes
Volume Number	48
Issue Number	3
e-ISSN	1572994X
Language	English
Publisher	Springer US
Publisher Date	2014-03-19
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	RstB2 protein Vibrio cholerae CTXϕ phage DNA-binding protein Single-stranded DNA Double-stranded DNA Medical Microbiology Virology Plant Sciences
Content Type	Text
Resource Type	Article
Subject	Virology Genetics Medicine Molecular Biology

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