Recombinant Escherichia coli Single-stranded DNA-binding protein (ssb)

1. Highly cooperative binding requires the 56 amino acid intrinsically disordered C-terminal linker (IDL) that connects the DNA binding domain with the 9 amino acid C-terminal acidic tip that is involved in SSB binding to other proteins involved in genome maintenance. PMID: 28782560
2. results indicate that SSB linker mutants are defective for SSB-SSB interactions, and when the IDL is removed a terminal SSB-DNA complex results. PMID: 28078720
3. a model wherein the IDL is responsible for mediating protein-protein interactions critical to each role. When interactions occur between SSB tetramers, cooperative binding to ssDNA results. When binding occurs between SSB and an interactome partner, storage or loading of that protein onto the DNA takes place. PMID: 28127816
4. Results support the idea that controlling the balance between SSB binding modes is critical for DNA Pol III holoenzyme stability. PMID: 25329071
5. this study shows that the amino acid composition and length of the intrinsically disordered linkers affects the ssDNA binding mode preferences of SSB protein. PMID: 25562210
6. The apparent diffusion coefficient of SSB ranged from 70,000 to 170,000nt(2)/s, which is at least 600 times higher than that determined from diffusion on short ssDNA oligomers, and is within the range reported for protein diffusion on double-stranded DNA. PMID: 24792418
7. Long-range electrostatic effects from the C-peptide may contribute more to regulating the activity of SSB than any engagement of the C-peptide by the single-stranded DNA-domain. PMID: 24606314
8. The results identify the binding site of the C-peptide on the OB-domain of the single-stranded DNA binding protein and show that most of the C-domain is highly flexible. PMID: 24288378
9. Authors provided evidence that the IntI1 integrase is able to counterbalance the observed effect of SSB on attC site folding. PMID: 24296671
10. These results indicate that a single SSB tetramer must interact simultaneously with multiple protein partners during some essential roles in genome maintenance. PMID: 24021816
11. In this study, chemical cross-linking, combined with high-mass matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS), is used to determine the stoichiometry of the SSB*ssDNA complex. PMID: 22549990
12. Steady-state kinetic experiments show that SSB stimulates ExoI activity through effects on both apparent k(cat) and K(m). PMID: 21572106
13. Study obtained experimental evidence of a reptation mechanism for protein movement along DNA wherein a protein slides via DNA bulge formation and propagation. PMID: 21784244
14. Mass spectrometric analysis of the chi subunit of DNA polymerase III cross-linked to a C-terminal peptide of SSB reveals that K132 of chi and D172 of SSB are in close contact. PMID: 20972214
15. single-stranded DNA binding is regulated by the C termini of Escherichia coli single-stranded DNA-binding (SSB) protein PMID: 20360609
16. SSB overexpression increases the stability of the (CAG)75 repeat array and leads to a loss of the bias towards large deletions for the same array. PMID: 19925793
17. DNA homopolymers and those lacking 8-oxopurines were less reactive toward DNA-SSB protein cross-links PMID: 15823024
18. the two major modes of SSB binding to DNA PMID: 17490681
19. Escherichia coli ssDNA-binding protein SSB limits access of RecA to ssDNA, DprA lowers this barrier. PMID: 17803906
20. Salt-dependent changes in the SSB protein significantly alter the stability of the protein-ssDNA complex. PMID: 18032436

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KEGG: ecj:JW4020

STRING: 316385.ECDH10B_4248