<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>10(7)</volume><submitter>Roy S</submitter><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</pubmed_abstract><journal>PloS one</journal><pagination>e0133843</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4521722</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Understanding the Physical and Molecular Basis of Stability of Arabidopsis DNA Pol λ under UV-B and High NaCl Stress.</pubmed_title><pmcid>PMC4521722</pmcid><pubmed_authors>Banerjee V</pubmed_authors><pubmed_authors>Roy S</pubmed_authors><pubmed_authors>Das KP</pubmed_authors></additional><is_claimable>false</is_claimable><name>Understanding the Physical and Molecular Basis of Stability of Arabidopsis DNA Pol λ under UV-B and High NaCl Stress.</name><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</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015</publication><modification>2025-04-05T00:04:59.624Z</modification><creation>2019-03-26T23:35:08Z</creation></dates><accession>S-EPMC4521722</accession><cross_references><pubmed>26230318</pubmed><doi>10.1371/journal.pone.0133843</doi></cross_references></HashMap>