Cross-linking of elongation factor EF-G to the 50S ribosomal subunit of Escherichia coli

A. Seetharama Acharya, P. B. Moore, F. M. Richards

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39 Scopus citations

Abstract

A wide variety of bifunctional protein reagents will covalently cross-link the elongation factor EF-G to the 50S ribosomal subunit of Escherichia coli. About 120,000 daltons of ribosomal proteins become cross-linked to EF-G upon extensive reaction. About 30,000 daltons of this material is made up of proteins L7 and L12 (mol wt 13,000 daltons). Thus, these two components, whose presence on the ribosome is required for the EF-G interaction, must be located at the EF-G binding site.

Original languageEnglish (US)
Pages (from-to)3108-3114
Number of pages7
JournalBiochemistry
Volume12
Issue number16
Publication statusPublished - 1973
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Acharya, A. S., Moore, P. B., & Richards, F. M. (1973). Cross-linking of elongation factor EF-G to the 50S ribosomal subunit of Escherichia coli. Biochemistry, 12(16), 3108-3114.