FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2088593314> ?p ?o ?g. }

• W2088593314 endingPage "23656" @default.
• W2088593314 startingPage "23644" @default.
• W2088593314 abstract "DNA primases catalyze the synthesis of oligoribonucleotides required for the initiation of lagging strand DNA synthesis. Prokaryotic primases consist of a zinc-binding domain (ZBD) necessary for recognition of a specific template sequence and a catalytic RNA polymerase domain. Interactions of both domains with the DNA template and ribonucleotides are required for primer synthesis. Five tryptophan residues are dispersed in the primase of bacteriophage T7: Trp-42 in the ZBD and Trp-69, -97, -147, and -255 in the RNA polymerase domain. Previous studies showed that replacement of Trp-42 with alanine in the ZBD decreases primer synthesis, whereas substitution of non-aromatic residues for Trp-69 impairs both primer synthesis and delivery. However, the roles of tryptophan at position 97, 147, or 255 remain elusive. To investigate the essential roles of these residues, we replaced each tryptophan with the structurally similar tyrosine and examined the effect of this subtle alteration on primer synthesis. The substitution at position 42, 97, or 147 reduced primer synthesis, whereas substitution at position 69 or 255 did not. The functions of the tryptophans were further examined at each step of primer synthesis. Alteration of residue 42 disturbed the conformation of the ZBD and resulted in partial loss of the zinc ion, impairing binding to the ssDNA template. Replacement of Trp-97 with tyrosine reduced the binding affinity to NTP and the catalysis step. The replacement of Trp-147 with tyrosine also impaired the catalytic step. Therefore, Trp-42 is important in maintaining the conformation of the ZBD for template binding; Trp-97 contributes to NTP binding and the catalysis step; and Trp-147 maintains the catalysis step.Background: What are the essential roles of five tryptophans in the T7 primase?Results: Replacement of Trp-42, -97, or -147 with the structurally similar tyrosine disturbs the conformation of the ZBD and reduces NTP binding and the catalysis step.Conclusion: Trp-42, -97, and -147 contribute to template binding, NTP binding, and the catalysis step.Significance: Trp-42, -97, and -147 play different but essential roles in T7 DNA primase. DNA primases catalyze the synthesis of oligoribonucleotides required for the initiation of lagging strand DNA synthesis. Prokaryotic primases consist of a zinc-binding domain (ZBD) necessary for recognition of a specific template sequence and a catalytic RNA polymerase domain. Interactions of both domains with the DNA template and ribonucleotides are required for primer synthesis. Five tryptophan residues are dispersed in the primase of bacteriophage T7: Trp-42 in the ZBD and Trp-69, -97, -147, and -255 in the RNA polymerase domain. Previous studies showed that replacement of Trp-42 with alanine in the ZBD decreases primer synthesis, whereas substitution of non-aromatic residues for Trp-69 impairs both primer synthesis and delivery. However, the roles of tryptophan at position 97, 147, or 255 remain elusive. To investigate the essential roles of these residues, we replaced each tryptophan with the structurally similar tyrosine and examined the effect of this subtle alteration on primer synthesis. The substitution at position 42, 97, or 147 reduced primer synthesis, whereas substitution at position 69 or 255 did not. The functions of the tryptophans were further examined at each step of primer synthesis. Alteration of residue 42 disturbed the conformation of the ZBD and resulted in partial loss of the zinc ion, impairing binding to the ssDNA template. Replacement of Trp-97 with tyrosine reduced the binding affinity to NTP and the catalysis step. The replacement of Trp-147 with tyrosine also impaired the catalytic step. Therefore, Trp-42 is important in maintaining the conformation of the ZBD for template binding; Trp-97 contributes to NTP binding and the catalysis step; and Trp-147 maintains the catalysis step. Background: What are the essential roles of five tryptophans in the T7 primase? Results: Replacement of Trp-42, -97, or -147 with the structurally similar tyrosine disturbs the conformation of the ZBD and reduces NTP binding and the catalysis step. Conclusion: Trp-42, -97, and -147 contribute to template binding, NTP binding, and the catalysis step. Significance: Trp-42, -97, and -147 play different but essential roles in T7 DNA primase." @default.
• W2088593314 created "2016-06-24" @default.
• W2088593314 creator A5011038929 @default.
• W2088593314 creator A5082077458 @default.
• W2088593314 creator A5085322583 @default.
• W2088593314 date "2012-07-01" @default.
• W2088593314 modified "2023-10-14" @default.
• W2088593314 title "The Roles of Tryptophans in Primer Synthesis by the DNA Primase of Bacteriophage T7" @default.
• W2088593314 cites W1659827168 @default.
• W2088593314 cites W1969717774 @default.
• W2088593314 cites W1969862311 @default.
• W2088593314 cites W1971044361 @default.
• W2088593314 cites W1975910300 @default.
• W2088593314 cites W1976786777 @default.
• W2088593314 cites W1985204165 @default.
• W2088593314 cites W1985907558 @default.
• W2088593314 cites W1998129350 @default.
• W2088593314 cites W2005760588 @default.
• W2088593314 cites W2005916059 @default.
• W2088593314 cites W2007438146 @default.
• W2088593314 cites W2008391101 @default.
• W2088593314 cites W2013916346 @default.
• W2088593314 cites W2019069746 @default.
• W2088593314 cites W2021914960 @default.
• W2088593314 cites W2023164122 @default.
• W2088593314 cites W2025938842 @default.
• W2088593314 cites W2026727321 @default.
• W2088593314 cites W2030475783 @default.
• W2088593314 cites W2037383718 @default.
• W2088593314 cites W2038994322 @default.
• W2088593314 cites W2044692297 @default.
• W2088593314 cites W2062875640 @default.
• W2088593314 cites W2065857906 @default.
• W2088593314 cites W2066894739 @default.
• W2088593314 cites W2068129156 @default.
• W2088593314 cites W2079881378 @default.
• W2088593314 cites W2087556720 @default.
• W2088593314 cites W2094186244 @default.
• W2088593314 cites W2094213518 @default.
• W2088593314 cites W2157271776 @default.
• W2088593314 cites W2212035881 @default.
• W2088593314 cites W4229608773 @default.
• W2088593314 doi "https://doi.org/10.1074/jbc.m112.366096" @default.
• W2088593314 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3390639" @default.
• W2088593314 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22605336" @default.
• W2088593314 hasPublicationYear "2012" @default.
• W2088593314 type Work @default.
• W2088593314 sameAs 2088593314 @default.
• W2088593314 citedByCount "10" @default.
• W2088593314 countsByYear W20885933142013 @default.
• W2088593314 countsByYear W20885933142015 @default.
• W2088593314 countsByYear W20885933142016 @default.
• W2088593314 countsByYear W20885933142018 @default.
• W2088593314 countsByYear W20885933142019 @default.
• W2088593314 countsByYear W20885933142020 @default.
• W2088593314 crossrefType "journal-article" @default.
• W2088593314 hasAuthorship W2088593314A5011038929 @default.
• W2088593314 hasAuthorship W2088593314A5082077458 @default.
• W2088593314 hasAuthorship W2088593314A5085322583 @default.
• W2088593314 hasBestOaLocation W20885933141 @default.
• W2088593314 hasConcept C104317684 @default.
• W2088593314 hasConcept C156719811 @default.
• W2088593314 hasConcept C178790620 @default.
• W2088593314 hasConcept C185592680 @default.
• W2088593314 hasConcept C194830204 @default.
• W2088593314 hasConcept C2756471 @default.
• W2088593314 hasConcept C2776165026 @default.
• W2088593314 hasConcept C2776706248 @default.
• W2088593314 hasConcept C2777563447 @default.
• W2088593314 hasConcept C515207424 @default.
• W2088593314 hasConcept C552990157 @default.
• W2088593314 hasConcept C55493867 @default.
• W2088593314 hasConcept C64241487 @default.
• W2088593314 hasConcept C67705224 @default.
• W2088593314 hasConcept C71240020 @default.
• W2088593314 hasConcept C82381507 @default.
• W2088593314 hasConcept C86803240 @default.
• W2088593314 hasConceptScore W2088593314C104317684 @default.
• W2088593314 hasConceptScore W2088593314C156719811 @default.
• W2088593314 hasConceptScore W2088593314C178790620 @default.
• W2088593314 hasConceptScore W2088593314C185592680 @default.
• W2088593314 hasConceptScore W2088593314C194830204 @default.
• W2088593314 hasConceptScore W2088593314C2756471 @default.
• W2088593314 hasConceptScore W2088593314C2776165026 @default.
• W2088593314 hasConceptScore W2088593314C2776706248 @default.
• W2088593314 hasConceptScore W2088593314C2777563447 @default.
• W2088593314 hasConceptScore W2088593314C515207424 @default.
• W2088593314 hasConceptScore W2088593314C552990157 @default.
• W2088593314 hasConceptScore W2088593314C55493867 @default.
• W2088593314 hasConceptScore W2088593314C64241487 @default.
• W2088593314 hasConceptScore W2088593314C67705224 @default.
• W2088593314 hasConceptScore W2088593314C71240020 @default.
• W2088593314 hasConceptScore W2088593314C82381507 @default.
• W2088593314 hasConceptScore W2088593314C86803240 @default.
• W2088593314 hasIssue "28" @default.
• W2088593314 hasLocation W20885933141 @default.
• W2088593314 hasLocation W20885933142 @default.
• W2088593314 hasLocation W20885933143 @default.

• next