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PMID: 1281451 Published · ppublish English Journal Article

Muscle-specific expression of SRF-related genes in the early embryo of Xenopus laevis.

The EMBO journal ·Vol. 11 ·No. 13 ·1992-12-00 ·Pages 4981-91

Chambers AE, Kotecha S, Towers N, Mohun TJ

Abstract

We have isolated two members of the RSRF protein family, SL-1 and SL-2, in Xenopus laevis. Both proteins contain SRF-type DNA binding domains and are related to the human protein, RSRFC4. SL-1 constitutes a novel member of the RSRF family whilst SL-2 is similar to human RSRFC4 throughout its length. SL-1 protein recognizes the consensus DNA sequence CTA(A/T)4TAR in vitro and can bind to the same regulatory sites as other A/T-rich sequence-specific binding activities, such as the muscle-specific regulatory factor, MEF-2. Transcription of both Xenopus genes is restricted to the somitic mesoderm of early embryos and subsequently to the body muscle (myotomes) of the tadpole. In contrast, both genes are expressed ubiquitously in the adult frog. A binding activity, antigenically related to both human RSRFC4 and the SL-2 gene product, is detected in Xenopus embryos and after gastrulation is localized to embryonic muscle. An indistinguishable binding activity is detected in many adult frog tissues. We conclude that the RSRF genes undergo a dramatic switch in their patterns of expression during development. We suggest that RSRF proteins may regulate muscle-specific transcription in embryos, but acquire other roles during the course of development.

Related Genes
RSRF SL-1 SL-2
MeSH Terms
Amino Acid Sequence Animals Base Sequence Blotting, Northern Culture Techniques DNA DNA-Binding Proteins/genetics,metabolism Gene Expression Humans In Situ Hybridization Mesoderm/metabolism Molecular Sequence Data Multigene Family Muscles/embryology,metabolism Protein Binding RNA/genetics Sequence Homology, Amino Acid Xenopus Proteins Xenopus laevis
Chemicals
DNA-Binding Proteins MEF2A protein, Xenopus MEF2D protein, Xenopus Xenopus Proteins RNA DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Chambers A E
Laboratory of Developmental Biochemistry, National Institute for Medical Research, Mill Hill, London, UK.
Kotecha S
Towers N
Mohun T J
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1992-12-00
Pages
4981-91
Language
English
Region
England
NLM ID
8208664
PMCID
PMC556976
Subset
IM
Databases
GENBANK
D13199, D13200, D13201, D13202, D13203, M94783, M94784, M94785, Z19123, Z19124
External Links
PubMed source PMC Full Text View journal details
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