TY - JOUR
AU - 
AB - Downloaded from genesdev.cshlp.org on October 25, 2021 - Published by Cold Spring Harbor Laboratory Press Human SRF-related proteins: DNA-binding properties and potential regulatory targets Roy Pollock and Richard Treisman Transcription Laboratory, Imperial Cancer Research Fund Laboratories, Lincoln's Inn Fields London WC2A 3PX, UK Serum response factor (SRF) is a transcription factor that binds the sequence CC(A/T)6GG found in a number of growth factor-inducible and muscle-specific promoters. We describe the isolation and characterization of cDNA clones encoding a family of three human SRF-related DNA-binding proteins. Each of these RSRF (related to SRF) proteins contains an 86-amino-acid amino-terminal region related to the SRF DNA-binding domain: In RSRFC4 and RSRFC9, this region is identical, whereas that present in RSRFR2 differs by seven conservative amino acid substitutions. The DNA-binding specificity of the RSRF proteins, which recognize the consensus sequence CTA(A/T)4TAG, is distinct from that of SRF. The entire RSRF common region is required for DNA binding, and the differential sequence specificity of the RSRFs and SRF is the result of differences in the basic amino-terminal part of this domain. The RSRF proteins bind DNA as dimers and can dimerize with one another but not with SRF. Although the RSRF mRNAs are expressed in 
TI - Human SRF-related proteins: DNA-binding properties and potential regulatory targets.
JF - Genes & Development
DO - 10.1101/gad.5.12a.2327
DA - 1991-12-01
UR - https://www.deepdyve.com/lp/unpaywall/human-srf-related-proteins-dna-binding-properties-and-potential-s6soR4c3ct
DP - DeepDyve
ER -