Bianco, Piero R and Pottinger, Sasheen and Tan, Hui Yin and Nguyenduc, Trong and Rex, Kervin and Varshney, Umesh (2017) The IDL of E-coli SSB links ssDNA and protein binding by mediating protein-protein interactions. In: PROTEIN SCIENCE, 26 (2). pp. 227-241.
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Abstract
The E. coli single strand DNA binding protein (SSB) is essential to viability where it functions in two seemingly disparate roles: it binds to single stranded DNA (ssDNA) and to target proteins that comprise the SSB interactome. The link between these roles resides in a previously under-appreciated region of the protein known as the intrinsically disordered linker (IDL). We present 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. The properties of the IDL that facilitate these interactions include the presence of repeats, a putative polyproline type II helix and, PXXP motifs that may facilitate direct binding to the OB-fold in a manner similar to that observed for SH3 domain binding of PXXP ligands in eukaryotic systems.
Item Type: | Journal Article |
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Publication: | PROTEIN SCIENCE |
Additional Information: | Copy right for this article belongs to the WILEY-BLACKWELL, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA |
Department/Centre: | Division of Biological Sciences > Microbiology & Cell Biology |
Date Deposited: | 03 Apr 2017 04:48 |
Last Modified: | 03 Apr 2017 04:48 |
URI: | http://eprints.iisc.ac.in/id/eprint/56445 |
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