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Gene Review:

lcrG - LcrG

Yersinia enterocolitica W22703

Lawton, D.G. et al., Neyt, C. et al., Boyd, A.P. et al., F??lker, S. et al., Iriarte, M. et al.

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Disease relevance of lcrG

Altered Ca2+ Regulation of Yop Secretion in Yersinia enterocolitica after DNA Adenine Methyltransferase Overproduction Is Mediated by Clp-Dependent Degradation of LcrG [1].

High impact information on lcrG

Two proteins, YopN and LcrG, are known to be involved in Yop-secretion control [2].
Translocation of these effectors across the eukaryotic cell membrane requires YopB, YopD and LcrG, but the mechanism is unclear [3].
Consistently, lysis of sheep erythrocytes was also dependent on YopB and YopD, but not on LcrG [3].
Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: requirement for translocators YopB and YopD, but not LcrG [3].
This demonstrated that binding of HeLa cells to purified LcrG is caused by heparan sulphate proteoglycans [4].

Chemical compound and disease context of lcrG

Heparin interferes with translocation of Yop proteins into HeLa cells and binds to LcrG, a regulatory component of the Yersinia Yop apparatus [4].

Analytical, diagnostic and therapeutic context of lcrG

In addition, comparisons of secretion patterns of effector proteins in Yersinia, arising from wild type and mutants of LcrV, support the proposed role of LcrG in titration of LcrV in vivo but also suggest that other factors may be involved [5].
We have purified recombinant LcrV, LcrG, and site-directed mutants of LcrV and demonstrated the structural integrity of these proteins using circular dichroism spectroscopy [5].

References

Altered Ca2+ Regulation of Yop Secretion in Yersinia enterocolitica after DNA Adenine Methyltransferase Overproduction Is Mediated by Clp-Dependent Degradation of LcrG. F??lker, S., Schmidt, M.A., Heusipp, G. J. Bacteriol. (2006) [Pubmed]
TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors. Iriarte, M., Sory, M.P., Boland, A., Boyd, A.P., Mills, S.D., Lambermont, I., Cornelis, G.R. EMBO J. (1998) [Pubmed]
Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: requirement for translocators YopB and YopD, but not LcrG. Neyt, C., Cornelis, G.R. Mol. Microbiol. (1999) [Pubmed]
Heparin interferes with translocation of Yop proteins into HeLa cells and binds to LcrG, a regulatory component of the Yersinia Yop apparatus. Boyd, A.P., Sory, M.P., Iriarte, M., Cornelis, G.R. Mol. Microbiol. (1998) [Pubmed]
Interactions of the type III secretion pathway proteins LcrV and LcrG from Yersinia pestis are mediated by coiled-coil domains. Lawton, D.G., Longstaff, C., Wallace, B.A., Hill, J., Leary, S.E., Titball, R.W., Brown, K.A. J. Biol. Chem. (2002) [Pubmed]

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