FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2007223824> ?p ?o ?g. }

• W2007223824 endingPage "708" @default.
• W2007223824 startingPage "699" @default.
• W2007223824 abstract "The major cold-shock protein of Bacillus subtilis, CspB, is a member of a protein family widespread among prokaryotes and eukaryotes that share the highly conserved cold-shock domain (CSD). The CSD domain is involved in transcriptional and translational regulation and was shown to bind the Y-box motif, a cis-element that contains the core sequence ATTGG, with high affinity. The three-dimensional structure of CspB, a prototype of this protein family, revealed that this hydrophilic CSD domain creates a surface rich in aromatic and basic amino acids that may act as the nucleic acid-binding site. We have analysed the potential role of conserved aromatic and basic residues in nucleic acid binding by site-directed mutagenesis. In gel retardation and ultraviolet cross-linking experiments, the ability of CspB mutants to bind single-stranded oligonucleotides (ssDNA) that contain the Y-box motif was investigated. Single substitutions of three highly conserved phenylalanine residues (Phe-15, Phe-17, Phe-27) by alanine and substitution of one histidine (His-29) by glutamine, all located within the putative RNA-binding sites RNP-1 and RNP-2, abolished the nucleic acid-binding activity of CspB. Conservative substitutions of Phe-15 to tyrosine (F15Y) showed a small increase in binding affinity, whereas separate replacement of Phe-17 and Phe-27 by tyrosine caused a reduction in binding activity. These and other substitutions including the conserved basic residues Lys-7, Lys-13 and Arg-56 as well as the aromatic residues Trp-8 and Phe-30 strongly suggest that CspB uses the sidechains of these amino acids for specific interaction with nucleic acids. Ultraviolet cross-linking experiments for CspB mutants with ssDNA supported the idea of specific CspB/nucleic acid interaction and indicated an essential role for the aromatic and basic residues in this binding. In addition, two-dimensional nuclear magnetic resonance studies with F17A, K13Q, F15Y and F27Y revealed that the mutants have the same overall structure as the wild-type CspB protein." @default.
• W2007223824 created "2016-06-24" @default.
• W2007223824 creator A5041775175 @default.
• W2007223824 creator A5051873783 @default.
• W2007223824 creator A5086706208 @default.
• W2007223824 creator A5088052021 @default.
• W2007223824 creator A5088345472 @default.
• W2007223824 date "1995-05-01" @default.
• W2007223824 modified "2023-09-23" @default.
• W2007223824 title "Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif" @default.
• W2007223824 cites W10876090 @default.
• W2007223824 cites W1552234482 @default.
• W2007223824 cites W1589353440 @default.
• W2007223824 cites W1866991149 @default.
• W2007223824 cites W1873683136 @default.
• W2007223824 cites W1900133438 @default.
• W2007223824 cites W1967506254 @default.
• W2007223824 cites W1967554461 @default.
• W2007223824 cites W1968360065 @default.
• W2007223824 cites W1968932730 @default.
• W2007223824 cites W1971341957 @default.
• W2007223824 cites W1971396838 @default.
• W2007223824 cites W1982110415 @default.
• W2007223824 cites W1983013658 @default.
• W2007223824 cites W1988299779 @default.
• W2007223824 cites W2000608709 @default.
• W2007223824 cites W2012828649 @default.
• W2007223824 cites W2027804115 @default.
• W2007223824 cites W2034890717 @default.
• W2007223824 cites W2037483793 @default.
• W2007223824 cites W2041852138 @default.
• W2007223824 cites W2044017204 @default.
• W2007223824 cites W2066328683 @default.
• W2007223824 cites W2068518785 @default.
• W2007223824 cites W2068663714 @default.
• W2007223824 cites W2072802762 @default.
• W2007223824 cites W2074122548 @default.
• W2007223824 cites W2074731613 @default.
• W2007223824 cites W2074756868 @default.
• W2007223824 cites W2080374811 @default.
• W2007223824 cites W2113443665 @default.
• W2007223824 cites W2122092321 @default.
• W2007223824 cites W2130920644 @default.
• W2007223824 cites W2135664793 @default.
• W2007223824 cites W2138270253 @default.
• W2007223824 cites W2140564918 @default.
• W2007223824 cites W2142626688 @default.
• W2007223824 cites W2150879617 @default.
• W2007223824 cites W2416851760 @default.
• W2007223824 doi "https://doi.org/10.1111/j.1365-2958.1995.tb02431.x" @default.
• W2007223824 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7476164" @default.
• W2007223824 hasPublicationYear "1995" @default.
• W2007223824 type Work @default.
• W2007223824 sameAs 2007223824 @default.
• W2007223824 citedByCount "135" @default.
• W2007223824 countsByYear W20072238242012 @default.
• W2007223824 countsByYear W20072238242013 @default.
• W2007223824 countsByYear W20072238242014 @default.
• W2007223824 countsByYear W20072238242015 @default.
• W2007223824 countsByYear W20072238242016 @default.
• W2007223824 countsByYear W20072238242017 @default.
• W2007223824 countsByYear W20072238242018 @default.
• W2007223824 countsByYear W20072238242019 @default.
• W2007223824 countsByYear W20072238242020 @default.
• W2007223824 countsByYear W20072238242021 @default.
• W2007223824 countsByYear W20072238242022 @default.
• W2007223824 crossrefType "journal-article" @default.
• W2007223824 hasAuthorship W2007223824A5041775175 @default.
• W2007223824 hasAuthorship W2007223824A5051873783 @default.
• W2007223824 hasAuthorship W2007223824A5086706208 @default.
• W2007223824 hasAuthorship W2007223824A5088052021 @default.
• W2007223824 hasAuthorship W2007223824A5088345472 @default.
• W2007223824 hasConcept C103408237 @default.
• W2007223824 hasConcept C104317684 @default.
• W2007223824 hasConcept C107824862 @default.
• W2007223824 hasConcept C129312508 @default.
• W2007223824 hasConcept C143065580 @default.
• W2007223824 hasConcept C156569929 @default.
• W2007223824 hasConcept C16318435 @default.
• W2007223824 hasConcept C199216141 @default.
• W2007223824 hasConcept C199677211 @default.
• W2007223824 hasConcept C24107716 @default.
• W2007223824 hasConcept C2776165026 @default.
• W2007223824 hasConcept C2777272437 @default.
• W2007223824 hasConcept C2777992278 @default.
• W2007223824 hasConcept C2779856020 @default.
• W2007223824 hasConcept C3017666073 @default.
• W2007223824 hasConcept C515207424 @default.
• W2007223824 hasConcept C523546767 @default.
• W2007223824 hasConcept C54355233 @default.
• W2007223824 hasConcept C552990157 @default.
• W2007223824 hasConcept C55493867 @default.
• W2007223824 hasConcept C67705224 @default.
• W2007223824 hasConcept C86339819 @default.
• W2007223824 hasConcept C86803240 @default.
• W2007223824 hasConcept C94966510 @default.
• W2007223824 hasConceptScore W2007223824C103408237 @default.
• W2007223824 hasConceptScore W2007223824C104317684 @default.

• next