Replication protein A3

{{Short description|Protein-coding gene in the species Homo sapiens}} {{Infobox_gene}} '''Replication protein A 14 kDa subunit''' is a protein that in humans is encoded by the ''RPA3'' gene.<ref name="pmid8454588">{{cite journal | vauthors = Umbricht CB, Erdile LF, Jabs EW, Kelly TJ | title = Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A | journal = The Journal of Biological Chemistry | volume = 268 | issue = 9 | pages = 6131–8 | date = Mar 1993 | doi = 10.1016/S0021-9258(18)53229-4 | pmid = 8454588 | doi-access = free }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RPA3 replication protein A3, 14kDa| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=6119}}</ref> RPA is a single-stranded DNA-binding protein that is conserved in eukaryotes and plays essential roles in the metabolism of nucleic acids.<ref>{{cite journal |last1=Salas |first1=Tonatiuh Romero |last2=Petruseva |first2=Irina |last3=Lavrik |first3=Olga |last4=Saintomé |first4=Carole |title=Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA |journal=Nucleic Acids Research |date=1 January 2009 |volume=37 |issue=1 |pages=38–46 |doi=10.1093/nar/gkn895 |doi-access=free |pmid=19010961 |pmc=2615627 }}</ref> Unlike helicase, RPA does not separate strands but binds and protects exposed single-stranded DNA to prevent secondary structure formation and degradation.<ref>{{cite journal |last1=Chen |first1=Ran |last2=Marc S |first2=Wold |title=Replication protein A: single-stranded DNA's first responder: dynamic DNA-interactions allow replication protein A to direct single-strand DNA intermediates into different pathways for synthesis or repair |journal=BioEssays: News and Reviews in Molecular, Cellular and Developmental Biology |date=2014 |volume=36,12 |issue=12 |pages=1156–1161 |doi=10.1002/bies.201400107 |pmid=25171654 |pmc=4629251 }}</ref> RPA is usually considered to be the functional equivalent of bacterial single-stranded DNA-binding proteins (SSB), although it is much more complex structurally in eukaryotic cells.<ref>{{cite journal |last1=Iftode |first1=C |last2=Daniely |first2=Y |last3=Borowiec |first3=J.A |title=Replication protein A (RPA): the eukaryotic SSB. |journal=Critical Reviews in Biochemistry and Molecular Biology |date=1999 |volume=34 |issue=3 |pages=141–180 |doi=10.1080/10409239991209255 |pmid=10473346 }}</ref>

== Interactions == RPA3 has been shown to interact with replication protein A1<ref name=pmid9461578>{{cite journal | vauthors = Bochkareva E, Frappier L, Edwards AM, Bochkarev A | title = The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain | journal=The Journal of Biological Chemistry | volume = 273 | issue = 7 | pages = 3932–6 | date = Feb 1998 | pmid = 9461578 | doi = 10.1074/jbc.273.7.3932 | doi-access = free }}</ref><ref name=pmid11927569>{{cite journal | vauthors = Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A | title = Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA | journal =The EMBO Journal | volume = 21 | issue = 7 | pages = 1855–63 | date = Apr 2002 | pmid = 11927569 | pmc = 125950 | doi = 10.1093/emboj/21.7.1855 }}</ref> and replication protein A2.<ref name=pmid9461578/><ref name=pmid11927569/> Together, they form a heterotrimeric complex that contributes to the direct binding of single-stranded DNA during replication, homologous recombination, nucleoetide excision repair, and mismatch repair.<ref>{{cite journal |last1=Madru |first1=C |last2=Martínez-Carranza |first2=M |title=A-binding mechanism and evolution of replication protein A |journal=Nature Communications |date=2023 |volume=14 |issue=1 |article-number=2326 |doi=10.1038/s41467-023-38048-w |pmid=37087464 |pmc=10122647 |bibcode=2023NatCo..14.2326M }}</ref> RPA3 can directly contact ssDNA on the 3' side of a substrate, and this polarity is crucial for the positioning and stability of nucleases that are involved in excision repair<ref>{{cite journal |last1=de Laat |first1=W. L |last2=Appeldoorn |first2=E |last3=Sugasawa |first3=K |last4=Weterings |first4=E |last5=Hoeijmakers |first5=J. H |last6=Jaspers |first6=N. G |title=DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair |journal=Genes & Development |date=15 August 1998 |volume=12 |issue=16 |pages=2598–2609 |doi=10.1101/gad.12.16.2598 |pmid=9716411 |pmc=317078 }}</ref>

== References == {{reflist}}

== Further reading == {{refbegin | 2}} * {{cite journal | vauthors = Iftode C, Daniely Y, Borowiec JA | title = Replication protein A (RPA): the eukaryotic SSB | journal = Critical Reviews in Biochemistry and Molecular Biology | volume = 34 | issue = 3 | pages = 141–80 | year = 1999 | pmid = 10473346 | doi = 10.1080/10409239991209255 }} * {{cite journal | vauthors = Keshav KF, Chen C, Dutta A | title = Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex | journal = Molecular and Cellular Biology | volume = 15 | issue = 6 | pages = 3119–28 | date = Jun 1995 | pmid = 7760808 | pmc = 230543 | doi = 10.1128/mcb.15.6.3119}} * {{cite journal | vauthors = Umbricht CB, Griffin CA, Hawkins AL, Grzeschik KH, O'Connell P, Leach R, Green ED, Kelly TJ | title = High-resolution genomic mapping of the three human replication protein A genes (RPA1, RPA2, and RPA3) | journal = Genomics | volume = 20 | issue = 2 | pages = 249–57 | date = Mar 1994 | pmid = 8020972 | doi = 10.1006/geno.1994.1161 | doi-access = free }} * {{cite journal | vauthors = Amacker M, Hottiger M, Mossi R, Hübscher U | title = HIV-1 nucleocapsid protein and replication protein A influence the strand displacement DNA synthesis of lentiviral reverse transcriptase | journal = AIDS | volume = 11 | issue = 4 | pages = 534–6 | date = Mar 1997 | pmid = 9084803 }} * {{cite journal | vauthors = Bochkareva E, Frappier L, Edwards AM, Bochkarev A | title = The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain | journal = The Journal of Biological Chemistry | volume = 273 | issue = 7 | pages = 3932–6 | date = Feb 1998 | pmid = 9461578 | doi = 10.1074/jbc.273.7.3932 | doi-access = free }} * {{cite journal | title = Toward a complete human genome sequence | journal = Genome Research | volume = 8 | issue = 11 | pages = 1097–108 | date = Nov 1998 | pmid = 9847074 | doi = 10.1101/gr.8.11.1097 | last1 = Sanger Centre | first1 = The | last2 = Washington University Genome Sequencing Cente | first2 = The | doi-access = free }} * {{cite journal | vauthors = Mer G, Bochkarev A, Gupta R, Bochkareva E, Frappier L, Ingles CJ, Edwards AM, Chazin WJ | title = Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA | journal = Cell | volume = 103 | issue = 3 | pages = 449–56 | date = Oct 2000 | pmid = 11081631 | doi = 10.1016/S0092-8674(00)00136-7 | s2cid = 16640087 | doi-access = free }} * {{cite journal | vauthors = Habel JE, Ohren JF, Borgstahl GE | title = Dynamic light-scattering analysis of full-length human RPA14/32 dimer: purification, crystallization and self-association | journal = Acta Crystallographica Section D | volume = 57 | issue = Pt 2 | pages = 254–9 | date = Feb 2001 | pmid = 11173472 | doi = 10.1107/S0907444900015225 | doi-access = | bibcode = 2001AcCrD..57..254H }} * {{cite journal | vauthors = Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A | title = Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA | journal = The EMBO Journal | volume = 21 | issue = 7 | pages = 1855–63 | date = Apr 2002 | pmid = 11927569 | pmc = 125950 | doi = 10.1093/emboj/21.7.1855 }} * {{cite journal | vauthors = Kneissl M, Pütter V, Szalay AA, Grummt F | title = Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells | journal = Journal of Molecular Biology | volume = 327 | issue = 1 | pages = 111–28 | date = Mar 2003 | pmid = 12614612 | doi = 10.1016/S0022-2836(03)00079-2 }} * {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R | s2cid = 4427026 }} * {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | article-number = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }} * {{cite journal | vauthors = Sankaranarayanan P, Schomay TE, Aiello KA, Alter O | title = Tensor GSVD of patient- and platform-matched tumor and normal DNA copy-number profiles uncovers chromosome arm-wide patterns of tumor-exclusive platform-consistent alterations encoding for cell transformation and predicting ovarian cancer survival | journal = PLOS ONE | volume = 10 | issue = 4 | article-number = e0121396 | date = April 2015 | pmid = 25875127 | doi = 10.1371/journal.pone.0121396 | id = [http://www.eurekalert.org/pub_releases/2015-04/uouh-nmi040915.php AAAS EurekAlert! Press Release] and [https://www.nae.edu/Projects/20730/wtop/134897.aspx NAE Podcast Feature] | pmc=4398562| bibcode = 2015PLoSO..1021396S | doi-access = free }} {{refend}}