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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| Published in | Biochemical journal Vol. 320 ( Pt 1); no. 1; pp. 247 - 252 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
15.11.1996
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| Subjects | |
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| 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. |
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| AbstractList | 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 (tRNAAsp**) in rebinding experiments, we could show that tRNA is selectively recaptured by the RNA-depleted vigilin-containing complex. 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 super(Asp*)*) in rebinding experiments, we could show that tRNA is selectively recaptured by the RNA-depleted vigilin-containing complex. 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. |
| Author | Kügler, S Grünweller, A Notbohm, H Purschke, W G Kruse, C Müller, P K |
| AuthorAffiliation | Department of Medical Molecular Biology, Medical University of Lübeck, Germany |
| AuthorAffiliation_xml | – name: Department of Medical Molecular Biology, Medical University of Lübeck, Germany |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/8947494$$D View this record in MEDLINE/PubMed |
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| Snippet | 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.... |
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| SubjectTerms | 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 |
| Title | Evidence for a novel cytoplasmic tRNA-protein complex containing the KH-multidomain protein vigilin |
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