Evidence for GroES acting as a transcriptional regulator

Biochemical and Biophysical Research Communications
G LegnameF Marcucci

Abstract

Cochaperonins (cpn10) assist chaperonins (cpn60) in promoting folding and assembly of other proteins. Upon expression of Mycobacterium tuberculosis cpn10 in Escherichia coli we have purified a polypeptide which, through amino acid sequencing, was identified as the endogenous E. coli 10K-S protein. Subsequent studies showed that its expression was specifically upregulated upon cloning of different members of the cpn10 family, including GroES, the E. coli cpn10. Pulse-chase experiments demonstrated that 10K-S is but one of several proteins whose expression is modulated upon cloning of cpn10. Up-regulation of 10K-S was also observed after exposure of normal cells, but not of groES- mutants, to elevated temperatures (42 degrees C). This allowed us to define 10K-S as a heat-shock protein (hsp) whose expression is dependent on the production of another hsp, GroES. Northern blot experiments showed that enhanced expression of 10K-S was consequent to increased accumulation of transcripts and that groES- mutants were devoid even of baseline levels of transcripts both at 37 degrees C and after temperature upshift. These results show that GroES, in addition to its established role in assisting protein folding may act as a transcriptional r...Continue Reading

Citations

Oct 28, 2016·Microbial Pathogenesis·Fernando Vargas-RomeroMauricio Castañón-Arreola
Jan 7, 2000·Journal of Molecular Biology·K S Gajiwala, S K Burley
Sep 8, 1998·Microbiology and Molecular Biology Reviews : MMBR·M K Berlyn

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