Molecular Biophysics Unit, Indian Institute of Science, Bangalore, Karnataka, India.
Department of Biochemistry, Indian Institute of Science, Bangalore, Karnataka, India.
IUBMB Life. 2018 Aug;70(8):786-794. doi: 10.1002/iub.1881.
Structure-specific helicases, such as RecG, play an important role in the resolution of recombination intermediates. A bioinformatic analysis of mycobacterial genomes led to the identification of a protein (RecG ) with a C-terminal "edge" domain, similar to the wedge domain of RecG. RecG is predominately found in the phylum Actinobacteria and in few human pathogens. Mycobacterium smegmatis RecG was able to bind branched DNA structures in vitro but failed to interact with single- or double-stranded DNA. The expression of recG in M. smegmatis cells was up-regulated during stationary phase/UV damage and down-regulated during MMS/H O treatment. These observations indicate the possible involvement of RecG in transactions during recombination events, that proceed though branched DNA intermediates. © 2018 IUBMB Life, 70(8):786-794, 2018.
结构特异性解旋酶，如 RecG，在重组中间体的解析中发挥重要作用。对分枝杆菌基因组的生物信息学分析导致鉴定出一种具有 C 末端“边缘”结构域的蛋白质（RecG），类似于 RecG 的楔形结构域。RecG 主要存在于放线菌门，少数人类病原体中也存在。分枝杆菌 RecG 能够在体外结合分支 DNA 结构，但不能与单链或双链 DNA 相互作用。RecG 在 M. smegmatis 细胞中的表达在静止期/UV 损伤时上调，在 MMS/H 2 O 处理时下调。这些观察结果表明 RecG 可能参与通过分支 DNA 中间体进行的重组事件中的交易。2018 年 IUBMB Life，70(8)：786-794，2018。
