Biochemical characterisation of UvrD helicase and RecJ exonuclease from Neisseria gonorrhoeae.

• Tác giả: Madhuraj Bhat, Debayan Ganguli, K C Manjunath, Desirazu N Rao
• Ngôn ngữ: eng
• Ký hiệu phân loại: 660.63 Biochemical engineering
• Thông tin xuất bản: Netherlands : International journal of biological macromolecules , 2025
• Bộ sưu tập: NCBI
• ID: 692897

Tóm tắt

UvrD helicase and RecJ exonuclease play a critical role in DNA repair and recombination process thereby involved in the maintenance of the genomic integrity. In addition to DNA repair pathways, UvrD helicase plays an important role in phase variation and maintenance of virulence in pathogenic bacteria while RecJ is a single-stranded DNA -specific 5'-3' exonuclease activity responsible for generating a long 3'ssDNA gap for DNA resynthesis by DNA ploymerases in mismatch repair (MMR). In spite of being vital for performing these functions, there have been few reports on the mismatch repair pathway in pathogenic bacteria and particularly the interplay of mismatch repair proteins in methylation independent mismatch repair. Purified UvrD helicase from Neisseria gonorrhoeae (FA1090) (NgoUvrD) exhibits 3'-5' polarity on ssDNA and unwinds blunt end duplex DNA as well as different DNA substrates with overhangs. While NgoUvrD binds to Ni