Department of Biochemistry, Indian Institute of Science, Bangalore, India.
FEBS Lett. 2020 Mar;594(5):851-863. doi: 10.1002/1873-3468.13671. Epub 2019 Nov 24.
The UvrABC excinuclease plays a vital role in bacterial nucleotide excision repair. While UvrA and UvrB subunits associate to form a UvrA B complex, interaction between UvrA and UvrC has not been demonstrated or quantified in any bacterial species. Here, using Mycobacterium tuberculosis UvrA (MtUvrA), UvrB (MtUvrB) and UvrC (MtUvrC) subunits, we show that MtUvrA binds to MtUvrB and equally well to MtUvrC with submicromolar affinity. Furthermore, MtUvrA forms a complex with MtUvrC both in vivo and in vitro, independently of DNA and UvrB. Collectively, these findings reveal new insights into the pairwise relationships between the subunits of the UvrABC incision complex.
UvrABC 外切核酸酶在细菌核苷酸切除修复中起着至关重要的作用。虽然 UvrA 和 UvrB 亚基结合形成 UvrA-B 复合物，但在任何细菌物种中都没有证明或量化 UvrA 和 UvrC 之间的相互作用。在这里，我们使用结核分枝杆菌 UvrA（MtUvrA）、UvrB（MtUvrB）和 UvrC（MtUvrC）亚基，表明 MtUvrA 以亚毫摩尔亲和力结合 MtUvrB 和 MtUvrC。此外，MtUvrA 在体内和体外均与 MtUvrC 形成复合物，独立于 DNA 和 UvrB。总之，这些发现揭示了 UvrABC 切口复合物亚基之间两两关系的新见解。
