SSBP_DROME
ID SSBP_DROME Reviewed; 146 AA.
AC P54622; Q5U164; Q9V3U4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Single-stranded DNA-binding protein, mitochondrial;
DE Short=Dm mtSSB;
DE Short=Mt-SSB;
DE Short=MtSSB;
DE AltName: Full=Protein low power;
DE Flags: Precursor;
GN Name=mtSSB; Synonyms=lopo; ORFNames=CG4337;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Oregon-R;
RX PubMed=10788480; DOI=10.1074/jbc.275.18.13628;
RA Ruiz de Mena I., Lefai E., Garesse R., Kaguni L.S.;
RT "Regulation of mitochondrial single-stranded DNA-binding protein gene
RT expression links nuclear and mitochondrial DNA replication in Drosophila.";
RL J. Biol. Chem. 275:13628-13636(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-146, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Ovary;
RX PubMed=8206370; DOI=10.1016/0378-1119(94)90093-0;
RA Stroumbakis N.D., Li Z., Tolias P.P.;
RT "RNA- and single-stranded DNA-binding (SSB) proteins expressed during
RT Drosophila melanogaster oogenesis: a homolog of bacterial and eukaryotic
RT mitochondrial SSBs.";
RL Gene 143:171-177(1994).
RN [6]
RP PROTEIN SEQUENCE OF 23-51, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MASS SPECTROMETRY.
RX PubMed=7673145; DOI=10.1074/jbc.270.36.21137;
RA Thommes P., Farr C.L., Marton R.F., Kaguni L.S., Cotterill S.;
RT "Mitochondrial single-stranded DNA-binding protein from Drosophila embryos.
RT Physical and biochemical characterization.";
RL J. Biol. Chem. 270:21137-21143(1995).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11294889; DOI=10.1091/mbc.12.4.821;
RA Maier D., Farr C.L., Poeck B., Alahari A., Vogel M., Fischer S.,
RA Kaguni L.S., Schneuwly S.;
RT "Mitochondrial single-stranded DNA-binding protein is required for
RT mitochondrial DNA replication and development in Drosophila melanogaster.";
RL Mol. Biol. Cell 12:821-830(2001).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF TRP-85 AND PHE-91.
RX PubMed=14754882; DOI=10.1074/jbc.m400283200;
RA Farr C.L., Matsushima Y., Lagina A.T. III, Luo N., Kaguni L.S.;
RT "Physiological and biochemical defects in functional interactions of
RT mitochondrial DNA polymerase and DNA-binding mutants of single-stranded
RT DNA-binding protein.";
RL J. Biol. Chem. 279:17047-17053(2004).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF 57-GLN-GLU-58; 74-TYR--ASN-76;
RP 100-LEU-GLU-101; 117-TYR--GLU-119 AND 123-GLN--GLY-125.
RX PubMed=21953457; DOI=10.1074/jbc.m111.289983;
RA Oliveira M.T., Kaguni L.S.;
RT "Reduced stimulation of recombinant DNA polymerase gamma and mitochondrial
RT DNA (mtDNA) helicase by variants of mitochondrial single-stranded DNA-
RT binding protein (mtSSB) correlates with defects in mtDNA replication in
RT animal cells.";
RL J. Biol. Chem. 286:40649-40658(2011).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF 74-TYR--ASN-76.
RX PubMed=26446790; DOI=10.1074/jbc.m115.673707;
RA Ciesielski G.L., Bermek O., Rosado-Ruiz F.A., Hovde S.L., Neitzke O.J.,
RA Griffith J.D., Kaguni L.S.;
RT "Mitochondrial Single-stranded DNA-binding Proteins Stimulate the Activity
RT of DNA Polymerase gamma by Organization of the Template DNA.";
RL J. Biol. Chem. 290:28697-28707(2015).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28318978; DOI=10.1016/j.cub.2017.02.014;
RA Yu Z., O'Farrell P.H., Yakubovich N., DeLuca S.Z.;
RT "The mitochondrial DNA polymerase promotes elimination of paternal
RT mitochondrial genomes.";
RL Curr. Biol. 27:1033-1039(2017).
CC -!- FUNCTION: Binds preferentially and cooperatively to pyrimidine rich
CC single-stranded DNA (ss-DNA) (PubMed:7673145, PubMed:8206370,
CC PubMed:21953457). Required to maintain the copy number of mitochondrial
CC DNA (mtDNA) and plays crucial roles during mtDNA replication that
CC stimulate activity of the gamma complex polymerase PolG1/tam at the
CC replication fork (PubMed:21953457, PubMed:26446790, PubMed:14754882,
CC PubMed:28318978, PubMed:7673145, PubMed:11294889). Promotes PolG1
CC activity largely by organizing the template DNA and eliminating
CC secondary structures to favor ss-DNA conformations that facilitate
CC PolG1 activity (PubMed:26446790, PubMed:21953457, PubMed:7673145).
CC {ECO:0000269|PubMed:11294889, ECO:0000269|PubMed:14754882,
CC ECO:0000269|PubMed:21953457, ECO:0000269|PubMed:26446790,
CC ECO:0000269|PubMed:28318978, ECO:0000269|PubMed:7673145,
CC ECO:0000269|PubMed:8206370}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7673145}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7673145}.
CC -!- TISSUE SPECIFICITY: Uniformly distributed in the early embryo. High
CC levels detected in the anterior and posterior midgut primordia of stage
CC 12 embryos. In larvae, high levels were detected in proliferating
CC tissues including the CNS and digestive tract. In adults, highly
CC expressed in the CNS, digestive tract and ovary.
CC {ECO:0000269|PubMed:10788480, ECO:0000269|PubMed:11294889,
CC ECO:0000269|PubMed:8206370}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Levels
CC are high during embryogenesis and in the larvae but decrease in the
CC pupae before increasing again in the adult.
CC {ECO:0000269|PubMed:10788480, ECO:0000269|PubMed:11294889,
CC ECO:0000269|PubMed:8206370}.
CC -!- MASS SPECTROMETRY: Mass=13845; Mass_error=14; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:7673145};
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the testes results in
CC a reduced number of paternal mitochondrial nucleoids at the nebenkern
CC stage of spermatogenesis (PubMed:28318978). However, the clearance of
CC nucleoids at the elongation stage of spermatogenesis is unaffected
CC (PubMed:28318978). {ECO:0000269|PubMed:28318978}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20507.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF16936.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF181084; AAF16936.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAF55287.2; -; Genomic_DNA.
DR EMBL; BT016028; AAV36913.2; -; mRNA.
DR EMBL; U00669; AAA20507.1; ALT_INIT; mRNA.
DR RefSeq; NP_536744.2; NM_080496.4.
DR AlphaFoldDB; P54622; -.
DR SMR; P54622; -.
DR BioGRID; 67018; 18.
DR DIP; DIP-22042N; -.
DR IntAct; P54622; 6.
DR MINT; P54622; -.
DR STRING; 7227.FBpp0099503; -.
DR PaxDb; P54622; -.
DR PRIDE; P54622; -.
DR DNASU; 41968; -.
DR EnsemblMetazoa; FBtr0083277; FBpp0082729; FBgn0010438.
DR GeneID; 41968; -.
DR KEGG; dme:Dmel_CG4337; -.
DR CTD; 41968; -.
DR FlyBase; FBgn0010438; mtSSB.
DR VEuPathDB; VectorBase:FBgn0010438; -.
DR eggNOG; KOG1653; Eukaryota.
DR GeneTree; ENSGT00390000002796; -.
DR HOGENOM; CLU_078758_2_1_1; -.
DR InParanoid; P54622; -.
DR OMA; GNCIGRF; -.
DR OrthoDB; 1304218at2759; -.
DR PhylomeDB; P54622; -.
DR BioGRID-ORCS; 41968; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 41968; -.
DR PRO; PR:P54622; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010438; Expressed in secondary oocyte and 32 other tissues.
DR Genevisible; P54622; DM.
DR GO; GO:0000262; C:mitochondrial chromosome; IDA:FlyBase.
DR GO; GO:0042645; C:mitochondrial nucleoid; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0090592; P:DNA synthesis involved in DNA replication; IDA:FlyBase.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:FlyBase.
DR GO; GO:0006264; P:mitochondrial DNA replication; IDA:UniProtKB.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IDA:UniProtKB.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:FlyBase.
DR GO; GO:1902394; P:positive regulation of exodeoxyribonuclease activity; IDA:FlyBase.
DR GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
DR GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; IMP:UniProtKB.
DR CDD; cd04496; SSB_OBF; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00984; SSB; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR011344; ssDNA-bd.
DR PANTHER; PTHR10302; PTHR10302; 1.
DR Pfam; PF00436; SSB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00621; ssb; 1.
DR PROSITE; PS50935; SSB; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA replication; DNA-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7673145"
FT CHAIN 23..146
FT /note="Single-stranded DNA-binding protein, mitochondrial"
FT /id="PRO_0000033268"
FT DOMAIN 38..142
FT /note="SSB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00252"
FT MUTAGEN 57..58
FT /note="QE->AA: In mtSSBloop12; significant reduction in
FT mitochondrial DNA copy number."
FT /evidence="ECO:0000269|PubMed:21953457"
FT MUTAGEN 74..76
FT /note="Missing: In mtSSBloop23; significant reduction in
FT mitochondrial DNA copy number. No effect on ability to
FT stimulate the activity of the polymerase PolG1."
FT /evidence="ECO:0000269|PubMed:21953457,
FT ECO:0000269|PubMed:26446790"
FT MUTAGEN 85
FT /note="W->A: Reduced DNA synthesis by the polymerase
FT PolG1."
FT /evidence="ECO:0000269|PubMed:14754882"
FT MUTAGEN 85
FT /note="W->T: Reduced DNA synthesis by the polymerase PolG1.
FT Severe decrease in the stimulation of DNA synthesis by the
FT polymerase PolG1 and decreased DNA binding; when associated
FT with A-91."
FT /evidence="ECO:0000269|PubMed:14754882"
FT MUTAGEN 85
FT /note="W->Y: No effect on DNA synthesis by the polymerase
FT PolG1."
FT /evidence="ECO:0000269|PubMed:14754882"
FT MUTAGEN 91
FT /note="F->A: No decrease in DNA synthesis by the polymerase
FT PolG1. Severe decrease DNA synthesis by the polymerase
FT PolG1 and decreased DNA binding; when associated with T-
FT 85."
FT /evidence="ECO:0000269|PubMed:14754882"
FT MUTAGEN 100..101
FT /note="LE->AA: In mtSSBalpha1; significant reduction in
FT mitochondrial DNA (mtDNA) copy number and reduced recovery
FT of mtDNA depletion induced by ethidium bromide."
FT /evidence="ECO:0000269|PubMed:21953457"
FT MUTAGEN 117..119
FT /note="YGE->AAA: In mtSSB45-1; significant reduction in
FT mitochondrial DNA (mtDNA) copy number and reduced recovery
FT of mtDNA depletion induced by ethidium bromide."
FT /evidence="ECO:0000269|PubMed:21953457"
FT MUTAGEN 123..125
FT /note="QQG->AAA: In mtSSB45-2; reduced mitochondrial DNA
FT (mtDNA) copy number and reduced recovery of mtDNA depletion
FT induced by ethidium bromide."
FT /evidence="ECO:0000269|PubMed:21953457"
SQ SEQUENCE 146 AA; 16368 MW; AD505175C0555D48 CRC64;
MQHTRRMLNP LLTGLRNLPA RGATTTTAAA PAKVEKTVNT VTILGRVGAD PQLRGSQEHP
VVTFSVATHT NYKYENGDWA QRTDWHRVVV FKPNLRDTVL EYLKKGQRTM VQGKITYGEI
TDQQGNQKTS TSIIADDVLF FRDANN
