InterPro : IPR000969

Name  Structure-specific recognition protein Short Name  SSrcognition
Type  Family Description  Human structure-specific recognition protein, SSRP1, []binds specifically to DNA modified with the anti-cancer drug cisplatin. An 81kDa protein is predicted, containing several highly-charged domains and a stretch of 75 residues that share 47% identity with a portion of the high mobility group (HMG) protein HMG1. This HMG box probably constitutes the structure recognition element for cisplatin-modified DNA, the probable recognition motif being the local duplex unwinding and bending that occurs on formation of intra-strand cross-links []. SSRP1 is the human homologue of a recently identified mouse protein that binds to recombination signal sequences []. These sequences have been postulated to form stem-loop structures, further implicating local bends and unwinding in DNA as a recognition target for HMG-box proteins. A Drosophila melanogastercDNA encoding an HMG-box-containing protein has also been isolated [, ]. This protein shares 50% sequence identity with human SSRP1. In vitro binding studies using Drosophila SSRP showed that the protein binds to single-stranded DNA and RNA, with highest affinity for nucleotides G and U. Comparison of the predicted amino acid sequences among SSRP family members reveals 48% identity, with structural conservation in the C terminus of the HMG box, as well as domains of highly charged residues. The most highly conserved regions lie in the poorly understood N terminus, suggesting that this portion of the protein is critical for its function [].This entry contains Pob3 , which is a subunit of the heterodimeric yeast FACT complex (Spt16p ()-Pob3p) []. The FACT complex facilitates RNA Polymerase II transcription elongation through nucleosomes by destabilising and then reassembling nucleosome structure [, ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

0 Parent Features

7 Publications

First Author Title Year Journal Volume Pages
Shirakata M HMG1-related DNA-binding protein isolated with V-(D)-J recombination signal probes. 1991 Mol Cell Biol 11 4528-36
Bruhn SL Isolation and characterization of cDNA clones encoding the Drosophila homolog of the HMG-box SSRP family that recognizes specific DNA structures. 1993 Nucleic Acids Res 21 1643-6
Bruhn SL Isolation and characterization of human cDNA clones encoding a high mobility group box protein that recognizes structural distortions to DNA caused by binding of the anticancer agent cisplatin. 1992 Proc Natl Acad Sci U S A 89 2307-11
Hsu T A Drosophila single-strand DNA/RNA-binding factor contains a high-mobility-group box and is enriched in the nucleolus. 1993 Proc Natl Acad Sci U S A 90 6488-92
Biswas D The yeast FACT complex has a role in transcriptional initiation. 2005 Mol Cell Biol 25 5812-22
Formosa T Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure. 2002 Genetics 162 1557-71
Belotserkovskaya R FACT facilitates transcription-dependent nucleosome alteration. 2003 Science 301 1090-3

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)