A cold-active heat-labile t-RNA modification GTPase from a psychrophilic bacterium Pseudomonas syringae (Lz4W)

Research in Microbiology
Ashish Kumar Singh, Sisinthy Shivaji

Abstract

A cold-active heat-labile t-RNA modification GTPase (TrmE) from psychrophilic bacterium Pseudomonas syringae (Lz4W) has been purified and characterized. The purified TrmE is a 53 kDa protein, has GTPase activity and hydrolyses only the oxy and deoxy forms of GTP but not the other nucleotide triphosphates. The enzyme exhibits optimal activity at 12-18 degrees C and retains 65% of its optimal activity at 4 degrees C, indicating that it is a cold-active enzyme. The enzyme is also heat-labile and loses 60% of its activity at 30 degrees C. This is the first report on the purification and characterization of a TrmE from a psychrophilic bacterium.

References

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Jul 18, 2002·The Journal of Biological Chemistry·William T Doerrler, Christian R H Raetz
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Jun 8, 2006·Annual Review of Biochemistry·Khawar Sohail Siddiqui, Ricardo Cavicchioli
May 12, 2009·Applied and Environmental Microbiology·Ashish K SinghS Shivaji

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Citations

Sep 3, 2011·Microbiology and Molecular Biology Reviews : MMBR·Natalie VerstraetenJan Michiels
Apr 25, 2014·Microbiology·Ashish Kumar SinghSisinthy Shivaji
Aug 26, 2014·Biochimica Et Biophysica Acta·Laura García-DescalzoCristina Cid
Aug 14, 2020·Genes·Ashley M EdwardsPatricia C Dos Santos
Nov 11, 2020·Environmental Microbiology·Theetha L PavankumarJohn E Hallsworth

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