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Gene Review:

copG - CopG

Streptococcus suis

del Solar, G. et al., Wales, T.E. et al., Acebo, P. et al., Takamatsu, D. et al., Acebo, P. et al., et al.

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High impact information on copG

The 5'-end and the levels of RNA II synthesized by pneumococcal cells harbouring the wild-type pLS1 or mutant plasmids (affected in either genes copG or rnaII) were analysed [1].
To determine the regulatory role of the two genes, we have cloned copG, rnaII or both elements at various gene dosages into pLS1-compatible plasmids [2].
Assays of incompatibility towards wild-type or mutant pLS1 plasmids showed that: (i) the rnaII gene product, rather than the DNA sequence encoding it, is responsible for the incompatibility, and (ii) CopG and RNA II act in trans and are able to correct up fluctuations in pLS1 copy number [2].
Binding of CopG to its operator results in repression, at the transcriptional level, of its own synthesis and that of the initiator of replication protein, RepB [3].
The guanidinium chloride-induced equilibrium unfolding properties of the wild-type CopG and (Y39W)CopG constructs in this work were characterized and used to develop a model for CopG's equilibrium unfolding reaction [4].

Biological context of copG

In this plasmid, the ORF1 (CopG protein) was preceded by two multiples of direct repeat and the conserved nucleotides that could be the double-strand origin (DSO) of rolling circle replication (RCR) mechanism [5].
A fluorescent CopG analog, (Y39W)CopG, was also designed and chemically synthesized to facilitate biophysical studies of CopG's protein folding and assembly reaction [4].
Molecular modeling of CopG showed a good fitting between the helix-turn-helix motifs of well-known repressor proteins and a bihelical unit of CopG [6].

Associations of copG with chemical compounds

The streptococcal plasmid pMV158 has been reported to harbor five genes: three involved in initiation of rolling circle replication and its control (copG, repB, and maII), one involved in conjugative mobilization (mobM), and the fifth one specifying constitutive resistance to tetracycline (tet) [7].

Other interactions of copG

ORF1 and ORF2 encode for proteins highly homologous to CopG and RepB of the pMV158 family, respectively [5].

Analytical, diagnostic and therapeutic context of copG

Circular dichroism measurements of CopG indicated a consensus average content of more than 50% alpha-helix and 10-35% beta-strand and turns, which is compatible with the predicted secondary structure of the protein [6].

References

Replication control of plasmid pLS1: the antisense RNA II and the compact rnaII region are involved in translational regulation of the initiator RepB synthesis. del Solar, G., Acebo, P., Espinosa, M. Mol. Microbiol. (1997) [Pubmed]
Replication control of plasmid pLS1: efficient regulation of plasmid copy number is exerted by the combined action of two plasmid components, CopG and RNA II. del Solar, G., Acebo, P., Espinosa, M. Mol. Microbiol. (1995) [Pubmed]
Plasmid transcriptional repressor CopG oligomerises to render helical superstructures unbound and in complexes with oligonucleotides. Costa, M., Solà, M., del Solar, G., Eritja, R., Hernández-Arriaga, A.M., Espinosa, M., Gomis-Rüth, F.X., Coll, M. J. Mol. Biol. (2001) [Pubmed]
Facile chemical synthesis and equilibrium unfolding properties of CopG. Wales, T.E., Richardson, J.S., Fitzgerald, M.C. Protein Sci. (2004) [Pubmed]
Sequence analysis of a small cryptic plasmid isolated from Streptococcus suis serotype 2. Takamatsu, D., Osaki, M., Sekizaki, T. Curr. Microbiol. (2000) [Pubmed]
Structural features of the plasmid pMV158-encoded transcriptional repressor CopG, a protein sharing similarities with both helix-turn-helix and beta-sheet DNA binding proteins. Acebo, P., García de Lacoba, M., Rivas, G., Andreu, J.M., Espinosa, M., del Solar, G. Proteins (1998) [Pubmed]
Identification of a new gene in the streptococcal plasmid pLS1: the rnaI gene. Acebo, P., Hernández-Arriaga, A.M., Kramer, M.G., Espinosa, M., del Solar, G. Plasmid (1998) [Pubmed]

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