Abstract
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.
MeSH Terms
Carrier Proteins
Cell Line
Chromatography, Affinity
Cytoplasm/metabolism
Electrophoresis, Polyacrylamide Gel
Humans
Proteins/pharmacology
RNA, Transfer/metabolism
RNA-Binding Proteins/biosynthesis,chemistry,metabolism
Chemicals
Carrier Proteins
Proteins
RNA-Binding Proteins
high density lipoprotein binding protein
RNA, Transfer
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Kruse C
Department of Medical Molecular Biology, Medical University of Lübeck, Germany.
Grünweller A
Notbohm H
Kügler S
Purschke W G
Müller P K
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