Cell
Volume 68, Issue 3, 7 February 1992, Pages 597-612
Journal home page for Cell

Article
Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element

https://doi.org/10.1016/0092-8674(92)90194-HGet rights and content

Abstract

We used a yeast genetic screen to isolate cDNAs that encode a protein, SRF accessory protein-1 (SAP-1), that is recruited to the c-fos serum response element (SRE) as part of a ternary complex that includes serum response factor (SRF). SAP-1 requires DNA-bound SRF for ternary complex formation and makes extensive DNA contacts to the 5′ side of SRF, but does not bind DNA autonomously. Ternary complex formation by SAP-1 requires only the DNA-binding domain of SRF, which can be replaced by that of the related yeast protein MCM1. We isolated cDNAs encoding two forms of SAP-1 protein, SAP-1a and SAP-1b, which differ at their C termini. Both SAP-1 proteins contain three regions of striking homology with the elk-1 protein, including an N-terminal ets domain. Ternary complex formation by SAP-1 requires both the ets domain and a second conserved region 50 amino acids to its C-terminal side. SAP-1 has similar DNA binding properties to the previously characterized HeLa cell protein p62TCF.

References (58)

  • R.K. Malik et al.

    Epidermal growth factor and other mitogens induce binding of a protein complex to the c-fos serum response element in human astrocytoma and other cells

    J. Biol. Chem.

    (1991)
  • C. Norman et al.

    Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element

    Cell

    (1988)
  • R.B. Pearson et al.

    Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations

    Meth. Enzymol.

    (1991)
  • P.E. Shaw et al.

    The ability of a ternary complex to form over the serum response element correlates with serum inducibility of the human c-fos promoter

    Cell

    (1989)
  • M.J. Sleigh

    A nonchromatographic assay for expression of the chloramphenicol acetyltransferase gene in eucaryotic cells

    Anal. Biochem.

    (1986)
  • S. Tan et al.

    DNA binding-induced conformational change of the yeast transcriptional activator PRTF

    Cell

    (1990)
  • J. Vieira et al.

    Production of single-stranded plasmid DNA

    Meth. Enzymol.

    (1987)
  • G. Ammerer

    Identification, purification, and cloning of a polypeptide (PRTF/GRM) that binds to mating-specific promoter elements in yeast

    Genes Dev.

    (1990)
  • A. Aruffo et al.

    Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system

  • L. Breeden et al.

    Regulation of the yeast HO gene

  • C.T. Chien et al.

    The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest

  • C. Christ et al.

    Functional domains of the yeast transcription/replication factor MCM1

    Genes Dev.

    (1991)
  • S. Dalton et al.

    A gene specific promoter element is required for optimal expression of the histone H1 gene in S-phase

    EMBO J.

    (1988)
  • B. Errede et al.

    STE12, a protein involved in cell-type-specific transcription and signal transduction in yeast, is part of protein-DNA complexes

    Genes Dev.

    (1989)
  • S. Fields et al.

    A novel genetic system to detect protein-protein interactions

    Nature

    (1989)
  • S.L. Forsburg et al.

    Identification and characterization of HAP4: a third component of the CCAAT-bound HAP2HAP3 heteromer

    Genes Dev.

    (1989)
  • M.A. Frohman

    Rapid amplification of cDNA ends (RACE): user friendly cDNA cloning

    Amplifications

    (1991)
  • C. Gauthier-Rouviere et al.

    Casein kinase II induces c-fos expression via the serum response element pathway and p67SRF phophorylation in living fibroblasts

    EMBO J.

    (1991)
  • C.R. Goding et al.

    Herpes simplex virus Vmw65-octamer binding protein interaction: a paradigm for combinatorial control of transcription

    Virology

    (1989)
  • Cited by (0)

    View full text