TY - JOUR
T1 - The tale of SSB
AU - Bianco, Piero R.
N1 - Funding Information:
Work in the Bianco laboratory is supported by NIH Grant GM100156 to PRB.
Publisher Copyright:
© 2016 Elsevier Ltd
PY - 2017/8
Y1 - 2017/8
N2 - The E. coli single stranded DNA binding protein (SSB) is essential to all aspects of DNA metabolism. Here, it has two seemingly disparate but equally important roles: it binds rapidly and cooperatively to single stranded DNA (ssDNA) and it binds to partner proteins that constitute the SSB interactome. These two roles are not disparate but are instead, intimately linked. A model is presented wherein the intrinsically disordered linker (IDL) is directly responsible for mediating protein-protein interactions. It does this by binding, via PXXP motifs, to the OB-fold (aka SH3 domain) of a nearby protein. When the nearby protein is another SSB tetramer, this leads to a highly efficient ssDNA binding reaction that rapidly and cooperatively covers and protects the exposed nucleic acid from degradation. Alternatively, when the nearby protein is a member of the SSB interactome, loading of the enzyme onto the DNA takes places.
AB - The E. coli single stranded DNA binding protein (SSB) is essential to all aspects of DNA metabolism. Here, it has two seemingly disparate but equally important roles: it binds rapidly and cooperatively to single stranded DNA (ssDNA) and it binds to partner proteins that constitute the SSB interactome. These two roles are not disparate but are instead, intimately linked. A model is presented wherein the intrinsically disordered linker (IDL) is directly responsible for mediating protein-protein interactions. It does this by binding, via PXXP motifs, to the OB-fold (aka SH3 domain) of a nearby protein. When the nearby protein is another SSB tetramer, this leads to a highly efficient ssDNA binding reaction that rapidly and cooperatively covers and protects the exposed nucleic acid from degradation. Alternatively, when the nearby protein is a member of the SSB interactome, loading of the enzyme onto the DNA takes places.
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U2 - 10.1016/j.pbiomolbio.2016.11.001
DO - 10.1016/j.pbiomolbio.2016.11.001
M3 - Review article
C2 - 27838363
AN - SCOPUS:85006797167
VL - 127
SP - 111
EP - 118
JO - Progress in Biophysics and Molecular Biology
JF - Progress in Biophysics and Molecular Biology
SN - 0079-6107
ER -