Evidence for a novel cytoplasmic tRNA-protein complex containing the KH-multidomain protein vigilin

Vigilin, a protein found predominantly in cells and tissues with a high biosynthetic capacity, was isolated in its native form from human HEp-2 cells (A.T.C.C. CCL23) by immunoaffinity chromatography. Vigilin forms part of a novel ribonucleoprotein complex that also contains additional, as yet uncha...

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Bibliographic Details
Published inBiochemical journal Vol. 320 ( Pt 1); no. 1; pp. 247 - 252
Main Authors Kruse, C, Grünweller, A, Notbohm, H, Kügler, S, Purschke, W G, Müller, P K
Format Journal Article
LanguageEnglish
Published England 15.11.1996
Subjects
Carrier Proteins
Cell Line
Chromatography, Affinity
Cytoplasm - metabolism
Electrophoresis, Polyacrylamide Gel
Humans
Proteins - pharmacology
RNA, Transfer - metabolism
RNA-Binding Proteins - biosynthesis
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - metabolism
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Summary:Vigilin, a protein found predominantly in cells and tissues with a high biosynthetic capacity, was isolated in its native form from human HEp-2 cells (A.T.C.C. CCL23) by immunoaffinity chromatography. Vigilin forms part of a novel ribonucleoprotein complex that also contains additional, as yet uncharacterized, proteins. Experimental evidence suggests that the nucleic acids entrapped in this complex are protected from RNase and belong to the tRNA family. Using either a pool of total human RNA or radioactively labelled tRNA (tRNA (Asp**)) in rebinding experiments, we could show that tRNA is selectively recaptured by the RNA-depleted vigilin-containing complex.
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ISSN:0264-6021
1470-8728
DOI:10.1042/bj3200247