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The mRNA‐binding protein COLBP is glutamate dehydrogenase
Author(s) -
Preiss Thomas,
Sang A.Elizabeth,
Chrzanowska-Lightowlers Zofia M.A.,
Lightowlers Robert N.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00569-u
Subject(s) - messenger rna , cytochrome c oxidase , glutamate dehydrogenase , biochemistry , microbiology and biotechnology , rna , untranslated region , binding site , chemistry , enzyme , biology , gene , glutamate receptor , receptor
Expression of the liver‐type isopeptides of cytochrome c oxidase is regulated post‐transcriptionally. An RNA‐binding activity has been found in only those cells where the liver‐type subunits are detected. This binding protein, termed COLBP, recognises sequences or structures within the 3′‐untranslated regions of transcripts encoding these liver‐type isopeptides and has been implicated in the modulation of mRNA expression. We now show by subcellular fractionation, immunocompetition, UV‐crosslinking and shift‐Western studies that the metabolic enzyme glutamate dehydrogenase, previously reported as being able to bind RNA, is the cytochrome c oxidase transcript‐binding protein, COLBP.