Cloning of human and rat cDNAs encoding the mitochondrial single-stranded DNA-binding protein (SSB)

Tiranti, Valeria; Rocchi, Mariano; DiDonato, Stefano; Zeviani, Massimo

doi:10.1016/0378-1119(93)90370-i

Cited by 107 publications

(80 citation statements)

References 33 publications

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“…We now show that NF-GMa is a complex of 42-and 22-kDa nuclear CSD proteins with a novel 16-kDa protein that forms on the noncoding (Ϫ) strand of the GM-CSF CK-1/CK-2 region in domain 1. We have determined the N-terminal sequence of the 16-kDa protein and found it to be identical to the N-terminal sequence of mature human mtSSB (44). Consistent with the properties of the 16-kDa protein, mtSSB has a molecular mass of 15.2 kDa and binds to single strand mitochondrial DNA (44,45).…”

Section: An Ordered Arrangement Of Repressor Elements Binding Csd Promentioning

confidence: 55%

“…We have determined the N-terminal sequence of the 16-kDa protein and found it to be identical to the N-terminal sequence of mature human mtSSB (44). Consistent with the properties of the 16-kDa protein, mtSSB has a molecular mass of 15.2 kDa and binds to single strand mitochondrial DNA (44,45). Human mtSSB belongs to a family of SSB proteins conserved from E. coli to mammals (44 -46, 73, 74).…”

Section: An Ordered Arrangement Of Repressor Elements Binding Csd Promentioning

confidence: 63%

“…Data base searches revealed that the sequence matched the N-terminal sequence of mature human mitochondrial single strand binding protein (mtSSB) (44). The mature human mtSSB binds to single strand DNA and is similar in size (15.2 kDa) to the 16-kDa component of the purified NF-GMa complex (44,45). SSB proteins have also been shown to be able to both homodimerize and heterodimerize (44, 46 -48).…”

Section: Nf-gma Represents a Higher Order Complex Of Csd Proteins Binmentioning

confidence: 94%

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An Ordered Array of Cold Shock Domain Repressor Elements across Tumor Necrosis Factor-responsive Elements of the Granulocyte-Macrophage Colony-stimulating Factor Promoter

Coles¹,

Diamond²,

Occhiodoro³

et al. 2000

Journal of Biological Chemistry

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The tumor necrosis factor-␣-responsive region of the human granulocyte-macrophage colony-stimulating factor (GM-CSF) promoter (؊114 to ؊31) encompasses binding sites for NF-B, CBF, AP-1, ETS, and NFAT families of transcription factors. We show both here and previously that mutation of any one of these binding sites greatly reduces tumor necrosis factor-␣ induction of the GM-CSF promoter. Interspersed between these elements are sequences that when mutated lead to an increase in GM-CSF promoter activity. We have previously shown that two of these repressor elements bind proteins known as cold shock domain (CSD) factors and that overexpression of CSD proteins leads to repression of GM-CSF promoter activity in fibroblasts. CSD proteins are single strand DNA-and RNA-binding proteins that contact 5-CCTG-3 sequences in the GM-CSF repressor elements. We show here that two newly identified repressor sequences in the proximal promoter can also bind CSD proteins. We have characterized the CSDcontaining protein complexes that bind to the GM-CSF promoter and identified a novel protein related to mitochondrial single strand binding protein that forms part of one of these complexes. The four CSD-binding sites on the promoter occur in pairs on opposite strands of the DNA and appear to form an ordered array of binding elements. A similar ordered array of CSD sites are present in the promoters of the granulocyte colony-stimulating factor and interleukin-3 genes, implying a common mechanism for negative regulation of these myeloid growth factors.

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Section: An Ordered Arrangement Of Repressor Elements Binding Csd Promentioning

confidence: 55%

Section: An Ordered Arrangement Of Repressor Elements Binding Csd Promentioning

confidence: 63%

Section: Nf-gma Represents a Higher Order Complex Of Csd Proteins Binmentioning

confidence: 94%

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An Ordered Array of Cold Shock Domain Repressor Elements across Tumor Necrosis Factor-responsive Elements of the Granulocyte-Macrophage Colony-stimulating Factor Promoter

Coles¹,

Diamond²,

Occhiodoro³

et al. 2000

Journal of Biological Chemistry

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“…Mitochondrial SSBs share similar physical and biochemical properties with E. coli SSB (5, 11, 18 -21), with which they exhibit a high degree of amino acid sequence conservation (21)(22)(23). Although high affinity DNA binding by SSBs can occur independently of other proteins, both functional and physical interactions between SSBs and a variety of enzymes involved in the above processes have been documented and, in particular, interactions between SSBs and replicative DNA polymerases have been demonstrated in bacterial, nuclear, and viral systems (17).…”

Section: Discussionmentioning

confidence: 99%

Physiological and Biochemical Defects in Functional Interactions of Mitochondrial DNA Polymerase and DNA-binding Mutants of Single-stranded DNA-binding Protein

Farr

Matsushima

Lagina

et al. 2004

Journal of Biological Chemistry

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Mitochondrial biogenesis is a key process in animal cell proliferation, and mtDNA replication is an essential component of that process. Whereas a large number of proteins participate in multi-component replication machines in bacterial and nuclear systems, a minimal set of essential proteins are likely involved in the mtDNA replication process (1). We have demonstrated functional interactions between the two-subunit Drosophila mitochondrial DNA polymerase (pol ␥) 1 and the homotetrameric mitochondrial single-stranded DNA-binding protein, mtSSB, at the levels of template-primer binding and initiation and elongation of DNA strand synthesis (2). These studies have documented roles for mtSSB in enhancing primer recognition and binding and in stimulation by 20-to 30-fold of the rate of initiation of DNA strands by pol ␥. Moreover, mtSSB increases severalfold the processivity of pol ␥ in DNA strand elongation.To probe further the biochemical and physiological importance of these functional interactions, we have evaluated the effects of altered forms of mtSSB on DNA binding per se and upon the coordinated reactions involving mtSSB and pol ␥. We find that even modest DNA-binding defects in mtSSB substantially affect DNA synthesis by pol ␥. Furthermore, under conditions that reduce cellular levels of endogenous wild-type mtSSB, a mtDNA depletion phenotype develops that is rescued by production of exogenous wild-type but not mutant mtSSB. EXPERIMENTAL PROCEDURESNucleotides and Nucleic Acids-Unlabeled deoxy-and ribonucleotides were purchased from Amersham Biosciences. [ 3 H]dTTP, [␣-32 P]dATP, and [␥-32 P]ATP were purchased from ICN Biochemicals. Wild-type (6,407 nucleotides (nt)) and recombinant (10,650 nt) M13 DNAs were prepared by standard laboratory methods. Oligodeoxynucleotides complementary to the M13 viral DNAs were synthesized in an Applied Biosystems oligonucleotide synthesizer. The primer for the recombinant M13 DNA that was used in the pol ␥ stimulation assay was 17 nt in length and the primer for the M13 wild-type DNA used in the processivity analysis was 15 nt in length. To prepare template primers for DNA synthesis, M13 DNAs were added to the 15-and 17-mer oligonucleotide primers to a concentration of ϳ70 mM (as nt, in 4-fold molar excess over homologous oligonucleotide), and the DNA mixtures were precipitated with ethanol. The pellets were resuspended in a buffer (0.1 ml) containing 10 mM Tris-HCl, pH 8.0, 0.3 M NaCl, and 0.03 M sodium citrate and were incubated at 65°C for 1 h, followed by incubation at 37°C for an additional hour to anneal the primer to the template. The sequence of the 38-mer oligonucleotide used in the DNA binding and gel mobility shift assays (GMSA) is complementary to positions 6291-6329 in M13mp7 DNA.Enzymes and Proteins-Drosophila DNA polymerase ␥ (Fraction VI, Ͼ90% homogeneous) was prepared from embryonic mitochondria, as described by Wernette and Kaguni (3). Recombinant Drosophila mtSSB (Ͼ90% homogeneous) was prepared as described by Farr et al. (2). T4 polynucleotide kinase and ...

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“…So far, three additional accessory factors are known to be involved in mtDNA synthesis. A single-stranded DNA-binding protein (mtSSB) has been reported (Tiranti et al, 1993), which is thought to bind to the single stranded parental H-strand to protect it. Furthermore mtDNA helicase activity has been reported for both vertebrates (bovine brain) (Hehman and Hauswirth, 1992) and invertebrates (sea urchin) (Roberti et al, 1996), and topoisomerases responsible for relaxing (type I) and introducing (type II) supercoils are involved in mtDNA replication (Kosovsky and Soslau, 1993;Castora and Simpson, 1979).…”

Section: Model(s) Of Replicationmentioning

confidence: 99%

Genetic aspects of mitochondrial genome evolution

Bernt

Braband

Schierwater

et al. 2013

Molecular Phylogenetics and Evolution

229

148

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Cloning of human and rat cDNAs encoding the mitochondrial single-stranded DNA-binding protein (SSB)

Cited by 107 publications

References 33 publications

An Ordered Array of Cold Shock Domain Repressor Elements across Tumor Necrosis Factor-responsive Elements of the Granulocyte-Macrophage Colony-stimulating Factor Promoter

An Ordered Array of Cold Shock Domain Repressor Elements across Tumor Necrosis Factor-responsive Elements of the Granulocyte-Macrophage Colony-stimulating Factor Promoter

Physiological and Biochemical Defects in Functional Interactions of Mitochondrial DNA Polymerase and DNA-binding Mutants of Single-stranded DNA-binding Protein

Genetic aspects of mitochondrial genome evolution

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