Mycobacterium tuberculosis UsfX (Rv3287c) exhibits novel nucleotide binding and hydrolysis properties

Biochemical and Biophysical Research Communications
Shuja Shafi MalikRavishankar Ramachandran

Abstract

The Mycobacterium tuberculosis UsfX protein is an anti-sigma factor which regulates its cognate sigma factor SigF. UsfX shares low sequence homology with other anti-sigma factors making it difficult to identify the nucleotide binding site and characterize its properties. We have identified that the NTP binding site occurs close to Trp106 and the area around the nucleotide binding site is predominantly negatively charged. UsfX binds to a variety of nucleotides unlike other reported anti-sigma factors and exhibits an unusual dual NTPase activity. In silico computational experiments have identified a XGSFS motif close to the nucleotide binding site for metal ion binding. This motif is analogous to the DXSXS motif reported earlier in the human integrin CR3 protein superfamily. Overall, the experiments suggest that the M. tuberculosis UsfX represents a distinct anti-sigma factor family with a novel nucleotide binding motif.

References

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Citations

Jun 15, 2010·Biochemical and Biophysical Research Communications·Ravi Kumar JaiswalB Gopal
Jan 10, 2009·Biochimica Et Biophysica Acta·Shuja Shafi MalikRavishankar Ramachandran
Jan 11, 2014·Journal of Receptor and Signal Transduction Research·Kiran Kumar MustyalaUma Vuruputuri
May 5, 2017·Journal of Molecular Recognition : JMR·Vikrant KumarSavita Yadav
Jan 11, 2018·Future Microbiology·Peifu ZhouJianping Xie

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