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PMID: 6708946 Published · ppublish English Journal Article

Affinity labelling of rat liver ribosomal protein S26 by heptauridylate containing a 5'-terminal alkylating group.

Molecular biology reports ·Vol. 9 ·No. 4 ·1984-01-00 ·Pages 219-22

Stahl J, Kobetz ND

Abstract

Heptauridylate bearing a radioactive alkylating [14C]-4-(N-2-chloroethyl-N-methylamino)benzylamine attached to the 5'-phosphate via amide bond, was bound to ribosomes and small ribosomal subunits from rat liver which thereby were coded to bind N-acylated Phe tRNA. After completion of the alkylating reaction and subsequent hydrolysis of the phosphamide bond ribosomal proteins were isolated. Radioactivity was found covalently associated preferentially with protein S26 and, to a very small extent, with proteins S3 and S3a. The affinity labelling reaction could be abolished by (pU)14 and poly(U). From the results it is concluded that ribosomal protein S26 is located at the mRNA binding site of rat liver ribosomes.

MeSH Terms
Affinity Labels Alkylating Agents Animals Binding Sites Poly U/analogs & derivatives,metabolism RNA, Messenger/metabolism Rats Ribosomal Proteins/metabolism Ribosomes/metabolism
Chemicals
Affinity Labels Alkylating Agents RNA, Messenger Ribosomal Proteins Poly U
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Stahl J
Kobetz N D
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23 references, click to expand
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Article Info
Journal
Molecular biology reports
Abbr.
Mol Biol Rep
ISSN
0301-4851
DOI
10.1007/BF00775350
Published
1984-01-00
Pages
219-22
Language
English
Region
Netherlands
NLM ID
0403234
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00775350 View journal details
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