Open AccessMycobacteriophage L 5 G p56, a novel member of the N rd H family of redoxins
Author(s) -
Kirtania Prithwiraj,
Bhattacharya Bidisha,
Das Gupta Sujoy K.
Publication year - 2014
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12502
Subject(s) - computational biology , chemistry , biology
Mycobacteriophage L5 gene 56 encodes a putative thioredoxin family protein. Phylogenetic analysis revealed that Gp56 and related proteins are distantly related to NrdH – a glutaredoxin homolog which has thioredoxin‐like properties. To understand its function, the recombinant version of the protein was biochemically characterized. For the sake of comparison, a mycobacterial thioredoxin, TrxB, was included in the study. Results show that Gp56 can be reduced by dithiothreitol, but only at a higher concentration as compared with TrxB, indicating that the standard redox potential of Gp56 is lower than that of TrxB. The reduced protein can subsequently act as a reductant of protein disulfide bonds. Gp56 can be reduced by NADPH with the help of thioredoxin reductase (TrxR) but less efficiently as compared with TrxB. The abilities of Gp56 and TrxB to reduce Gp50, the L5‐encoded ribonucleotide reductase, was examined. While both are capable of executing this function, the former needs more reducing equivalents in the process as compared with the latter. This study shows that L5Gp56 represents a new class of NrdH‐like proteins that function optimally in a reducing environment.