FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2080170863> ?p ?o ?g. }

• W2080170863 endingPage "4543" @default.
• W2080170863 startingPage "4534" @default.
• W2080170863 abstract "Replication protein A (RPA) is a heterotrimeric single-stranded DNA-binding protein that is essential for DNA metabolism. Human RPA is composed of subunits of 70, 32, and 14 kDa with intrinsic DNA-binding activity localized to the 616-amino acid, 70-kDa subunit (RPA70). We have made a series of C-terminal deletions to map the functional domains of RPA70. Deletion of the C terminus resulted in polypeptides that were significantly more soluble than RPA70 but were unable to form stable complexes with the other two subunits of RPA. These data suggest that the C-terminal region of RPA70 may be important for complex formation. The DNA-binding domain was localized to a region of RPA70 between residues 1 and 441. A mutant containing residues 1-441 bound oligonucleotides with an intrinsic affinity close to wild-type RPA complex. This mutant also appeared to bind with reduced cooperativity. We conclude that the C terminus of RPA70 and the 32- and 14-kDa subunits are not involved directly with interactions with DNA but may have a role in cooperativity of RPA binding. RPA70 deletion mutants were not able to support DNA replication even in the presence of a complex of the 32- and 14-kDa subunits, suggesting that the heterotrimeric complex is essential for DNA replication. The putative zinc finger in the C terminus of RPA70 is not required for single-stranded DNA-binding activity. Replication protein A (RPA) is a heterotrimeric single-stranded DNA-binding protein that is essential for DNA metabolism. Human RPA is composed of subunits of 70, 32, and 14 kDa with intrinsic DNA-binding activity localized to the 616-amino acid, 70-kDa subunit (RPA70). We have made a series of C-terminal deletions to map the functional domains of RPA70. Deletion of the C terminus resulted in polypeptides that were significantly more soluble than RPA70 but were unable to form stable complexes with the other two subunits of RPA. These data suggest that the C-terminal region of RPA70 may be important for complex formation. The DNA-binding domain was localized to a region of RPA70 between residues 1 and 441. A mutant containing residues 1-441 bound oligonucleotides with an intrinsic affinity close to wild-type RPA complex. This mutant also appeared to bind with reduced cooperativity. We conclude that the C terminus of RPA70 and the 32- and 14-kDa subunits are not involved directly with interactions with DNA but may have a role in cooperativity of RPA binding. RPA70 deletion mutants were not able to support DNA replication even in the presence of a complex of the 32- and 14-kDa subunits, suggesting that the heterotrimeric complex is essential for DNA replication. The putative zinc finger in the C terminus of RPA70 is not required for single-stranded DNA-binding activity." @default.
• W2080170863 created "2016-06-24" @default.
• W2080170863 creator A5065806062 @default.
• W2080170863 creator A5087322488 @default.
• W2080170863 date "1995-03-01" @default.
• W2080170863 modified "2023-09-30" @default.
• W2080170863 title "Structural Analysis of Human Replication Protein A" @default.
• W2080170863 cites W1484383644 @default.
• W2080170863 cites W152730474 @default.
• W2080170863 cites W1533565768 @default.
• W2080170863 cites W1539182448 @default.
• W2080170863 cites W1550656265 @default.
• W2080170863 cites W1554226644 @default.
• W2080170863 cites W1554850792 @default.
• W2080170863 cites W1558614105 @default.
• W2080170863 cites W1559981481 @default.
• W2080170863 cites W1570295242 @default.
• W2080170863 cites W1574197136 @default.
• W2080170863 cites W1574209182 @default.
• W2080170863 cites W1578842363 @default.
• W2080170863 cites W1590134197 @default.
• W2080170863 cites W1594126558 @default.
• W2080170863 cites W159450053 @default.
• W2080170863 cites W1605838085 @default.
• W2080170863 cites W1659681861 @default.
• W2080170863 cites W1828636759 @default.
• W2080170863 cites W1873199501 @default.
• W2080170863 cites W1967902178 @default.
• W2080170863 cites W1970456889 @default.
• W2080170863 cites W1972653649 @default.
• W2080170863 cites W1983134926 @default.
• W2080170863 cites W1988939915 @default.
• W2080170863 cites W1989054182 @default.
• W2080170863 cites W1995806503 @default.
• W2080170863 cites W1999632568 @default.
• W2080170863 cites W2001586358 @default.
• W2080170863 cites W2004669805 @default.
• W2080170863 cites W2006206801 @default.
• W2080170863 cites W2014142607 @default.
• W2080170863 cites W2024434976 @default.
• W2080170863 cites W2025504171 @default.
• W2080170863 cites W2027324850 @default.
• W2080170863 cites W2027697827 @default.
• W2080170863 cites W2035746057 @default.
• W2080170863 cites W2040159897 @default.
• W2080170863 cites W2049221234 @default.
• W2080170863 cites W2055348937 @default.
• W2080170863 cites W2060850037 @default.
• W2080170863 cites W2067154171 @default.
• W2080170863 cites W2067223250 @default.
• W2080170863 cites W2068761725 @default.
• W2080170863 cites W2082523354 @default.
• W2080170863 cites W2094014256 @default.
• W2080170863 cites W2100584834 @default.
• W2080170863 cites W2100837269 @default.
• W2080170863 cites W2139768549 @default.
• W2080170863 cites W2142844417 @default.
• W2080170863 cites W2159847993 @default.
• W2080170863 cites W2189281745 @default.
• W2080170863 cites W282058052 @default.
• W2080170863 cites W4246528186 @default.
• W2080170863 cites W4293247451 @default.
• W2080170863 cites W4379250860 @default.
• W2080170863 cites W838635636 @default.
• W2080170863 doi "https://doi.org/10.1074/jbc.270.9.4534" @default.
• W2080170863 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7876222" @default.
• W2080170863 hasPublicationYear "1995" @default.
• W2080170863 type Work @default.
• W2080170863 sameAs 2080170863 @default.
• W2080170863 citedByCount "83" @default.
• W2080170863 countsByYear W20801708632012 @default.
• W2080170863 countsByYear W20801708632013 @default.
• W2080170863 countsByYear W20801708632014 @default.
• W2080170863 countsByYear W20801708632015 @default.
• W2080170863 countsByYear W20801708632016 @default.
• W2080170863 countsByYear W20801708632017 @default.
• W2080170863 countsByYear W20801708632019 @default.
• W2080170863 countsByYear W20801708632021 @default.
• W2080170863 countsByYear W20801708632022 @default.
• W2080170863 crossrefType "journal-article" @default.
• W2080170863 hasAuthorship W2080170863A5065806062 @default.
• W2080170863 hasAuthorship W2080170863A5087322488 @default.
• W2080170863 hasBestOaLocation W20801708631 @default.
• W2080170863 hasConcept C104292427 @default.
• W2080170863 hasConcept C104317684 @default.
• W2080170863 hasConcept C107824862 @default.
• W2080170863 hasConcept C113271649 @default.
• W2080170863 hasConcept C139407321 @default.
• W2080170863 hasConcept C151158763 @default.
• W2080170863 hasConcept C153911025 @default.
• W2080170863 hasConcept C166014724 @default.
• W2080170863 hasConcept C187250156 @default.
• W2080170863 hasConcept C188036394 @default.
• W2080170863 hasConcept C22840021 @default.
• W2080170863 hasConcept C25166345 @default.
• W2080170863 hasConcept C5179208 @default.
• W2080170863 hasConcept C552990157 @default.
• W2080170863 hasConcept C55468747 @default.

• next