{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10(7)"],"submitter":["Roy S"],"pubmed_abstract":["Here, we have investigated the physical and molecular basis of stability of Arabidopsis DNA Pol λ, the sole X family DNA polymerase member in plant genome, under UV-B and salinity stress in connection with the function of the N-terminal BRCT (breast cancer-associated C terminus) domain and Ser-Pro rich region in the regulation of the overall structure of this protein. Tryptophan fluorescence studies, fluorescence quenching and Bis-ANS binding experiments using purified recombinant full length Pol λ and its N-terminal deletion forms have revealed UV-B induced conformational change in BRCT domain deficient Pol λ. On the other hand, the highly conserved C-terminal catalytic core PolX domain maintained its tertiary folds under similar condition. Circular dichroism (CD) and fourier transform in"],"journal":["PloS one"],"pagination":["e0133843"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4521722"],"repository":["biostudies-literature"],"pubmed_title":["Understanding the Physical and Molecular Basis of Stability of Arabidopsis DNA Pol λ under UV-B and High NaCl Stress."],"pmcid":["PMC4521722"],"pubmed_authors":["Banerjee V","Roy S","Das KP"],"additional_accession":[]},"is_claimable":false,"name":"Understanding the Physical and Molecular Basis of Stability of Arabidopsis DNA Pol λ under UV-B and High NaCl Stress.","description":"Here, we have investigated the physical and molecular basis of stability of Arabidopsis DNA Pol λ, the sole X family DNA polymerase member in plant genome, under UV-B and salinity stress in connection with the function of the N-terminal BRCT (breast cancer-associated C terminus) domain and Ser-Pro rich region in the regulation of the overall structure of this protein. Tryptophan fluorescence studies, fluorescence quenching and Bis-ANS binding experiments using purified recombinant full length Pol λ and its N-terminal deletion forms have revealed UV-B induced conformational change in BRCT domain deficient Pol λ. On the other hand, the highly conserved C-terminal catalytic core PolX domain maintained its tertiary folds under similar condition. Circular dichroism (CD) and fourier transform in","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015","modification":"2025-04-05T00:04:59.624Z","creation":"2019-03-26T23:35:08Z"},"accession":"S-EPMC4521722","cross_references":{"pubmed":["26230318"],"doi":["10.1371/journal.pone.0133843"]}}