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Phylogenetic distribution, structural analysis and interaction of nucleotide excision repair proteins in cyanobacteria.
Singh, Prashant R; Gupta, Amit; Pathak, Jainendra; Sinha, Rajeshwar P.
Affiliation
  • Singh PR; Laboratory of Photobiology and Molecular Microbiology, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi 221005, India.
  • Gupta A; Laboratory of Photobiology and Molecular Microbiology, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi 221005, India.
  • Rajneesh; Laboratory of Photobiology and Molecular Microbiology, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi 221005, India.
  • Pathak J; Laboratory of Photobiology and Molecular Microbiology, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi 221005, India.
  • Sinha RP; Laboratory of Photobiology and Molecular Microbiology, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi 221005, India; University Center for Research & Development (UCRD), Chandigarh University, India. Electronic address: rpsinhabhu@gmail.com.
DNA Repair (Amst) ; 126: 103487, 2023 06.
Article de En | MEDLINE | ID: mdl-37054651
ABSTRACT
Cyanobacteria are photosynthetic Gram-negative, oxygen evolving prokaryotes with cosmopolitan distribution. Ultraviolet radiation (UVR) and other abiotic stresses result in DNA lesions in cyanobacteria. Nucleotide excision repair (NER) pathway removes the DNA lesions produced by UVR to normal DNA sequence. In cyanobacteria, detailed knowledge about NER proteins is poorly studied. Therefore, we have studied the NER proteins in cyanobacteria. Analyses of 289 amino acids sequence from 77 cyanobacterial species have revealed the presence of a minimum of one copy of NER protein in their genome. Phylogenetic analysis of NER protein shows that UvrD has maximal rate of amino acid substitutions which resulted in increased branch length. The motif analysis shows that UvrABC proteins is more conserved than UvrD, Further, UvrA with UvrB protein interacts with each other and form stable complex which have DNA binding domain on the surface of the complex. UvrB also have DNA binding domain. Positive electrostatic potential was found in the DNA binding region, which is followed by negative and neutral electrostatic potential. Additionally, the surface accessibility values at the DNA strands of T5-T6 dimer binding site were maximal. Protein nucleotide interaction shows the strong binding of T5-T6 dimer with NER proteins of Synechocystis sp. PCC 6803. This process repairs the UV-induced DNA lesions in dark when photoreactivation is inactive. Regulation of NER proteins protect cyanobacterial genome and maintain the fitness of organism under different abiotic stresses.
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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Cyanobactéries / Protéines Escherichia coli Langue: En Journal: DNA Repair (Amst) Sujet du journal: BIOLOGIA MOLECULAR / BIOQUIMICA Année: 2023 Type de document: Article Pays d'affiliation: Inde

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Cyanobactéries / Protéines Escherichia coli Langue: En Journal: DNA Repair (Amst) Sujet du journal: BIOLOGIA MOLECULAR / BIOQUIMICA Année: 2023 Type de document: Article Pays d'affiliation: Inde