Immunochemical accessibility of ribosomal protein S4 in the 30 S ribosome. The interaction of S4 with S5 and S12

Donald Winkelmann, Lawrence Kahan

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The reactivity of protein S4-specific antibody preparations with 30 S ribosomal subunits and intermediates of in vitro subunit reconstitution has been characterized using a quantitative antibody binding assay. Anti-S4 antibody preparations did not react with native 30 S ribosomal subunits; however, they did react with various subunit assembly intermediates that lacked proteins S5 and S12. The inclusion of proteins S5 and S12 in reconstituted particles resulted in a large decrease in anti-S4 reactivity, and it was concluded that proteins S5 and S12 are primarily responsible for the masking of S4 antigenic determinants in the 30 S subunit. The effect of S5 and S12 on S4 accessibility is consistent with data from a variety of other approaches, suggesting that these proteins form a structural and functional domain in the small ribosomal subunit.

Original languageEnglish (US)
Pages (from-to)357-374
Number of pages18
JournalJournal of molecular biology
Volume165
Issue number2
DOIs
StatePublished - Apr 5 1983
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology

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