Evidence for a Novel Cytoplasmic TRNA-protein Complex Containing the KH-multidomain Protein Vigilin

Overview

Journal Biochem J

Specialty Biochemistry

Date 1996 Nov 15

PMID 8947494

Citations 13

Authors

C Kruse

A Grunweller

H Notbohm

S Kugler

W G Purschke

P K Muller

Affiliations

Soon will be listed here.

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.

Citing Articles

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Scp160p is required for translational efficiency of codon-optimized mRNAs in yeast.

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Vigilin interacts with signal peptide peptidase.

Lu S, Jeon A, Schmitt-Ulms G, Qamar S, Dodd R, McDonald B Proteome Sci. 2012; 10(1):33.

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Long-term culture of a cell population from Siberian sturgeon (Acipenser baerii) head kidney.

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