Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism.
| dc.contributor.author | Deed, Richard W | |
| dc.contributor.author | Jasiok, Michelle | |
| dc.contributor.author | Norton, John D | |
| dc.date.accessioned | 2010-04-06T08:52:18Z | |
| dc.date.available | 2010-04-06T08:52:18Z | |
| dc.date.issued | 1996-09-09 | |
| dc.identifier.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. | en |
| dc.identifier.issn | 0014-5793 | |
| dc.identifier.pmid | 8804437 | |
| dc.identifier.doi | 10.1016/0014-5793(96)00868-X | |
| dc.identifier.uri | http://hdl.handle.net/10541/95596 | |
| dc.description.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. | |
| dc.language.iso | en | en |
| dc.subject | Cancer Proteins | en |
| dc.subject.mesh | Adult | |
| dc.subject.mesh | Alternative Splicing | |
| dc.subject.mesh | B-Lymphocytes | |
| dc.subject.mesh | Blotting, Northern | |
| dc.subject.mesh | Cells, Cultured | |
| dc.subject.mesh | Gene Expression | |
| dc.subject.mesh | Genetic Variation | |
| dc.subject.mesh | Helix-Loop-Helix Motifs | |
| dc.subject.mesh | Humans | |
| dc.subject.mesh | Inhibitor of Differentiation Proteins | |
| dc.subject.mesh | Neoplasm Proteins | |
| dc.subject.mesh | RNA | |
| dc.subject.mesh | Transcription Factors | |
| dc.title | Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism. | en |
| dc.type | Article | en |
| dc.contributor.department | CRC Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, UK. grgrwd@picr.cr.man.ac.uk | en |
| dc.identifier.journal | FEBS Letters | en |
| html.description.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. |