Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism.

2.50
Hdl Handle:
http://hdl.handle.net/10541/95596
Title:
Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism.
Authors:
Deed, Richard W; Jasiok, Michelle; Norton, John D
Abstract:
The Id family of helix-loop-helix proteins function as negative regulators of DNA binding, basic helix-loop-helix proteins in the regulation of cell growth and differentiation. We report here on the identification of a 17 kDa variant of the 14 kDa Id-3 protein termed Id-3L (long version) which possesses a unique 60 amino acid carboxy-terminus generated by read through of a 'coding intron' and alternative splicing. Northern analysis revealed expression of a minor 1.1 kb Id-3L transcript together with the predominant 0.95 kb Id-3 transcript in the majority of adult human tissues analysed. The variant Id-3L protein is functionally distinguishable from conventional Id-3 since in in vitro DNA mobility shift assays, it was greatly impaired in its ability to abrogate binding of the basic helix-loop-helix protein, E47, to an E box recognition sequence.
Affiliation:
CRC Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, UK. grgrwd@picr.cr.man.ac.uk
Citation:
Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism. 1996, 393 (1):113-6 FEBS Lett.
Journal:
FEBS Letters
Issue Date:
9-Sep-1996
URI:
http://hdl.handle.net/10541/95596
DOI:
10.1016/0014-5793(96)00868-X
PubMed ID:
8804437
Type:
Article
Language:
en
ISSN:
0014-5793
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorDeed, Richard Wen
dc.contributor.authorJasiok, Michelleen
dc.contributor.authorNorton, John Den
dc.date.accessioned2010-04-06T08:52:18Z-
dc.date.available2010-04-06T08:52:18Z-
dc.date.issued1996-09-09-
dc.identifier.citationAttenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism. 1996, 393 (1):113-6 FEBS Lett.en
dc.identifier.issn0014-5793-
dc.identifier.pmid8804437-
dc.identifier.doi10.1016/0014-5793(96)00868-X-
dc.identifier.urihttp://hdl.handle.net/10541/95596-
dc.description.abstractThe Id family of helix-loop-helix proteins function as negative regulators of DNA binding, basic helix-loop-helix proteins in the regulation of cell growth and differentiation. We report here on the identification of a 17 kDa variant of the 14 kDa Id-3 protein termed Id-3L (long version) which possesses a unique 60 amino acid carboxy-terminus generated by read through of a 'coding intron' and alternative splicing. Northern analysis revealed expression of a minor 1.1 kb Id-3L transcript together with the predominant 0.95 kb Id-3 transcript in the majority of adult human tissues analysed. The variant Id-3L protein is functionally distinguishable from conventional Id-3 since in in vitro DNA mobility shift assays, it was greatly impaired in its ability to abrogate binding of the basic helix-loop-helix protein, E47, to an E box recognition sequence.en
dc.language.isoenen
dc.subjectCancer Proteinsen
dc.subject.meshAdult-
dc.subject.meshAlternative Splicing-
dc.subject.meshB-Lymphocytes-
dc.subject.meshBlotting, Northern-
dc.subject.meshCells, Cultured-
dc.subject.meshGene Expression-
dc.subject.meshGenetic Variation-
dc.subject.meshHelix-Loop-Helix Motifs-
dc.subject.meshHumans-
dc.subject.meshInhibitor of Differentiation Proteins-
dc.subject.meshNeoplasm Proteins-
dc.subject.meshRNA-
dc.subject.meshTranscription Factors-
dc.titleAttenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism.en
dc.typeArticleen
dc.contributor.departmentCRC Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, UK. grgrwd@picr.cr.man.ac.uken
dc.identifier.journalFEBS Lettersen

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