Apparent association constants for E. coli ribosomal proteins S4, S7, S8, S15, S17 and S20 binding to 16S RNA

Jean Schwarzbauer, Gary R. Craven

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

We have previously reported the development of a technique utilizing nitrocellulose filters, which rapidly separates ribosomal protein-ribosomal RNA complexes from unbound protein1, 2. We have used this technique to obtain binding data for the association of proteins S4, S7, S8, S15, S17 and S20 with 16SRNA. With the exception of protein S17, the association behavior for each of these proteins exhibits a single binding site with a unique binding constant. The apparent association constants have been calculated and have been found to have a range from 1.6 × 106M-1for protein S7 to7.1 × 107M-1for protein S17. The Scatchard plot for the protein S17 binding data is biphasic, suggesting that within the RNA population two different binding sites exist, each with a different apparent association constant.

Original languageEnglish (US)
Pages (from-to)2223-2237
Number of pages15
JournalNucleic acids research
Volume9
Issue number9
DOIs
StatePublished - May 11 1981
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Genetics

Fingerprint Dive into the research topics of 'Apparent association constants for E. coli ribosomal proteins S4, S7, S8, S15, S17 and S20 binding to 16S RNA'. Together they form a unique fingerprint.

Cite this