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Gene Review:

repA - hypothetical protein

Escherichia coli

Jezewska, M.J. et al., Noirot-Gros, M.F. et al., Ziegelin, G. et al., Spiers, A.J. et al., Kantor, A. et al., et al.

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Disease relevance of repA

For replication of a circular PY54 minimal replicon that has been derived from a linear minireplicon, two phage-encoded loci are essential in Escherichia coli: (i) the reading frame of the replication initiation gene repA and (ii) its 212-bp origin located within the 3' portion of repA [1].
The largest open reading frame encodes a protein similar to the replication protein, RepA, found in pAB49 from Acinetobacter baumannii and pNI10 from Pseudomonas [2].

High impact information on repA

Mutation analysis of the rolling circle (RC) replication initiator protein RepA of plasmid pC194 was targeted to tyrosine and acidic amino acids (glutamate and aspartate) which are well conserved among numerous related plasmids [3].
We propose that the active site of RepA contains two different catalytic centers, corresponding to a tyrosine and a glutamate [3].
In this aspect, the RepA helicase is different from the Escherichia coli DnaB hexamer that shows large preference for purine homo-oligomers [4].
However, these assays suggest that the transcriptional responses of orip and repAp to RepA repression are significantly different, despite the fact that both promoters are embedded within the BCDD'D" repeat elements [5].
The 68 amino acid carrier region was a block of three polypeptides consisting of a truncated RepA, a synthetic cellulose binding domain and a hexa histidine domain [6].

Biological context of repA

CbpA acted in an ATP-dependent reaction with DnaK and GrpE to remodel inactive dimers of plasmid P1 RepA into monomers active in P1 DNA binding [7].
Sequencing analysis revealed a non-coding region, repA, spanning the first 440 bp, followed by an open reading frame, repB, encoding a putative protein of 390 amino acids [8].
Thus, a region essential for efficient activation of the replication origin was assigned to the P1 RepA molecule as well as to the Rts1 RepA molecule [9].

Analytical, diagnostic and therapeutic context of repA

Interactions between the replicative RepA helicase hexamer of plasmid RSF1010 with the single-stranded DNA (ssDNA) have been studied, using the quantitative fluorescence titration, analytical sedimentation velocity, and sedimentation equilibrium techniques [4].

References

The repA gene of the linear Yersinia enterocolitica prophage PY54 functions as a circular minimal replicon in Escherichia coli. Ziegelin, G., Tegtmeyer, N., Lurz, R., Hertwig, S., Hammerl, J., Appel, B., Lanka, E. J. Bacteriol. (2005) [Pubmed]
A novel neisserial shuttle plasmid: a useful new tool for meningococcal research. O' Dwyer, C.A., Langford, P.R., Kroll, J.S. FEMS Microbiol. Lett. (2005) [Pubmed]
Active site of the replication protein of the rolling circle plasmid pC194. Noirot-Gros, M.F., Bidnenko, V., Ehrlich, S.D. EMBO J. (1994) [Pubmed]
Interactions of the RepA helicase hexamer of plasmid RSF1010 with the ssDNA. Quantitative analysis of stoichiometries, intrinsic affinities, cooperativities, and heterogeneity of the total ssDNA-binding site. Jezewska, M.J., Galletto, R., Bujalowski, W. J. Mol. Biol. (2004) [Pubmed]
Regulatory interactions between RepA, an essential replication protein, and the DNA repeats of RepFIB from plasmid P307. Spiers, A.J., Bhana, N., Bergquist, P.L. J. Bacteriol. (1993) [Pubmed]
Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria. Zhang, L., Falla, T., Wu, M., Fidai, S., Burian, J., Kay, W., Hancock, R.E. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM. Chae, C., Sharma, S., Hoskins, J.R., Wickner, S. J. Biol. Chem. (2004) [Pubmed]
Molecular characterization of the replicon of the Pediococcus pentosaceus 43200 pediocin A plasmid pMD136. Kantor, A., Montville, T.J., Mett, A., Shapira, R. FEMS Microbiol. Lett. (1997) [Pubmed]
Functional domains of Rts1 and P1 RepA proteins for initiation of replication. Li, Y.F., Hayashi, T., Terawaki, Y. Plasmid (1998) [Pubmed]

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