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SpGCF1, a sea urchin embryo DNA-binding protein, exists as five nested variants encoded by a single mRNA.

Abstract：

:Several Strongylocentrotus purpuratus gene cis-regulatory regions contain asymmetric C4 sequences which are core elements of target sites for a specific DNA-protein interaction. Blastula stage nuclear extract contains five proteins which specifically bind to these target sites, resulting in a characteristic pattern of complexes in gel mobility shift assays. We used automated affinity chromatography to purify a protein which binds to these sites and have isolated the corresponding cDNA. This protein, SpGCF1, is a novel sea urchin DNA-binding protein with no overall homology to proteins reported in the databases currently available. The DNA-binding domain of this protein was identified by a deletion analysis. As demonstrated both for protein translated in vitro and for bacterial protein expressed from a cDNA clone, a single SpGCF1 mRNA serves as a template for the synthesis of five DNA-binding polypeptides. We show that these five polypeptides are most likely produced by differential usage of a nested set of AUG start codons in the SpGCF1 cDNA and thus contain variable amounts of a proline-rich N-terminal domain. Since proline-rich regions often serve as transcriptional activation domains, the five SpGCF1 proteins apparently possess different "activation potentials."

journal_name

Dev Biol

journal_title

Developmental biology

authors

Zeller RW,Coffman JA,Harrington MG,Britten RJ,Davidson EH

doi

10.1006/dbio.1995.1181

subject

Has Abstract

pub_date

1995-06-01 00:00:00

pages

713-27

issue

2

eissn

0012-1606

issn

1095-564X

pii

S0012-1606(85)71181-5

journal_volume

169

pub_type

杂志文章

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