Characterization and regulation of the protein binding to a cis-acting element, RET 1, in the rat opsin promoter

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

RET 1 is a binding site for retinal nuclear proteins located at -136 to -110 bp in the rat opsin promoter, as defined by DNase protection assays. A similar sequence is found in the upstream flanking regions of many other photoreceptor genes in mammals and other species, including Drosophila. A 7-base consensus sequence, CAATTAG, is found in these genes and has the binding activity of the longer RET 1 element. A 40-kDa protein that binds to RET 1 has been purified over 2 × 105-fold to apparent homogeneity by affinity chromatography. The RET 1 binding activity is first detectable at E18 and increases during the first two postnatal weeks. At embryonic ages the retarded bands show an altered mobility and at early postnatal ages two bands are detected, with the adult band increasing and the embryonic band decreasing in intensity. Treatment of early postnatal retinas with bFGF increased the binding activity in nuclear extracts and caused a shift in migration of the retarded band to a position characteristic of the embryonic form of the complex. The results support the hypothesis that RET 1-like elements play an important role in rod photoreceptor development.

Original languageEnglish (US)
Pages (from-to)259-271
Number of pages13
JournalJournal of Molecular Neuroscience
Volume5
Issue number4
DOIs
StatePublished - Jan 1 1994

Fingerprint

Opsins
Protein Binding
Rats
Genes
Retinal Rod Photoreceptor Cells
Affinity chromatography
Mammals
Deoxyribonucleases
Consensus Sequence
Nuclear Proteins
Affinity Chromatography
Drosophila
Retina
Assays
Binding Sites
Proteins

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Genetics
  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

@article{fa46bf147ca24ee686e403d04ae72b90,
title = "Characterization and regulation of the protein binding to a cis-acting element, RET 1, in the rat opsin promoter",
abstract = "RET 1 is a binding site for retinal nuclear proteins located at -136 to -110 bp in the rat opsin promoter, as defined by DNase protection assays. A similar sequence is found in the upstream flanking regions of many other photoreceptor genes in mammals and other species, including Drosophila. A 7-base consensus sequence, CAATTAG, is found in these genes and has the binding activity of the longer RET 1 element. A 40-kDa protein that binds to RET 1 has been purified over 2 × 105-fold to apparent homogeneity by affinity chromatography. The RET 1 binding activity is first detectable at E18 and increases during the first two postnatal weeks. At embryonic ages the retarded bands show an altered mobility and at early postnatal ages two bands are detected, with the adult band increasing and the embryonic band decreasing in intensity. Treatment of early postnatal retinas with bFGF increased the binding activity in nuclear extracts and caused a shift in migration of the retarded band to a position characteristic of the embryonic form of the complex. The results support the hypothesis that RET 1-like elements play an important role in rod photoreceptor development.",
author = "Xiu Yu and Colin Barnstable",
year = "1994",
month = "1",
day = "1",
doi = "10.1007/BF02736726",
language = "English (US)",
volume = "5",
pages = "259--271",
journal = "Journal of Molecular Neuroscience",
issn = "0895-8696",
publisher = "Humana Press",
number = "4",

}

TY - JOUR

T1 - Characterization and regulation of the protein binding to a cis-acting element, RET 1, in the rat opsin promoter

AU - Yu, Xiu

AU - Barnstable, Colin

PY - 1994/1/1

Y1 - 1994/1/1

N2 - RET 1 is a binding site for retinal nuclear proteins located at -136 to -110 bp in the rat opsin promoter, as defined by DNase protection assays. A similar sequence is found in the upstream flanking regions of many other photoreceptor genes in mammals and other species, including Drosophila. A 7-base consensus sequence, CAATTAG, is found in these genes and has the binding activity of the longer RET 1 element. A 40-kDa protein that binds to RET 1 has been purified over 2 × 105-fold to apparent homogeneity by affinity chromatography. The RET 1 binding activity is first detectable at E18 and increases during the first two postnatal weeks. At embryonic ages the retarded bands show an altered mobility and at early postnatal ages two bands are detected, with the adult band increasing and the embryonic band decreasing in intensity. Treatment of early postnatal retinas with bFGF increased the binding activity in nuclear extracts and caused a shift in migration of the retarded band to a position characteristic of the embryonic form of the complex. The results support the hypothesis that RET 1-like elements play an important role in rod photoreceptor development.

AB - RET 1 is a binding site for retinal nuclear proteins located at -136 to -110 bp in the rat opsin promoter, as defined by DNase protection assays. A similar sequence is found in the upstream flanking regions of many other photoreceptor genes in mammals and other species, including Drosophila. A 7-base consensus sequence, CAATTAG, is found in these genes and has the binding activity of the longer RET 1 element. A 40-kDa protein that binds to RET 1 has been purified over 2 × 105-fold to apparent homogeneity by affinity chromatography. The RET 1 binding activity is first detectable at E18 and increases during the first two postnatal weeks. At embryonic ages the retarded bands show an altered mobility and at early postnatal ages two bands are detected, with the adult band increasing and the embryonic band decreasing in intensity. Treatment of early postnatal retinas with bFGF increased the binding activity in nuclear extracts and caused a shift in migration of the retarded band to a position characteristic of the embryonic form of the complex. The results support the hypothesis that RET 1-like elements play an important role in rod photoreceptor development.

UR - http://www.scopus.com/inward/record.url?scp=0028700947&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028700947&partnerID=8YFLogxK

U2 - 10.1007/BF02736726

DO - 10.1007/BF02736726

M3 - Article

C2 - 7577368

AN - SCOPUS:0028700947

VL - 5

SP - 259

EP - 271

JO - Journal of Molecular Neuroscience

JF - Journal of Molecular Neuroscience

SN - 0895-8696

IS - 4

ER -