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PMID: 3637121 Published · ppublish English Journal Article

Eukaryotic pre-tRNA 5' processing nuclease: copurification with a complex cylindrical particle.

Cell ·Vol. 46 ·No. 3 ·1986-08-01 ·Pages 377-85

Castaño JG, Ornberg R, Koster JG, Tobian JA, Zasloff M

Abstract

In eukaryotes pre-tRNA species are processed at the 5' end by an endonuclease. Here we describe the first characterization of the structure of a eukaryotic pre-tRNA 5' processing endonuclease. The 5' pre-tRNAase, isolated from X. laevis ovaries, copurifies with a 16S macromolecular complex consisting of at least 14 polypeptides ranging in MW from about 20,000 to 32,000. These polypeptides comprise a cylindrical particle, apparently organized as a stack of four rings, similar or identical to a ubiquitous eukaryotic subcellular particle described in the literature over the past 15 years. Similar copurification is observed for the enzyme from HeLa cells, suggesting that the X. laevis enzyme is representative of a general class of eukaryotic pre-tRNA 5' processing nuclease.

MeSH Terms
Animals Cell Nucleus/enzymology,ultrastructure Endoribonucleases/isolation & purification,metabolism Female HeLa Cells/enzymology,ultrastructure Humans Nucleic Acid Precursors/metabolism Ovary/enzymology,ultrastructure Peptides/isolation & purification RNA Precursors RNA, Transfer, Amino Acyl/metabolism RNA, Transfer, Met RNA, Transfer, Phe Xenopus laevis/metabolism
Chemicals
Nucleic Acid Precursors Peptides RNA Precursors RNA, Transfer, Amino Acyl RNA, Transfer, Met RNA, Transfer, Phe pre-tRNA(Met) pre-tRNA(Phe) Endoribonucleases 5'-pre-tRNA endonuclease
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Castaño J G
Ornberg R
Koster J G
Tobian J A
Zasloff M
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
1986-08-01
Pages
377-85
Language
English
Region
United States
NLM ID
0413066
Subset
IM
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