Cross-Linking of Elongation Factor EF-G to the 50S Ribosomal Subunit of Escherichia coli

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

doi:10.1021/bi00740a026

Cross-Linking of Elongation Factor EF-G to the 50S Ribosomal Subunit of Escherichia coli

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

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	3108-3114
Number of pages	7
Journal	Biochemistry
Volume	12
Issue number	16
DOIs	https://doi.org/10.1021/bi00740a026
State	Published - Jul 1 1973
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

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10.1021/bi00740a026

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title = "Cross-Linking of Elongation Factor EF-G to the 50S Ribosomal Subunit of Escherichia coli",

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.",

author = "Acharya, {A. Seetharama} and Moore, {P. B.} and Richards, {F. M.}",

year = "1973",

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AU - Acharya, A. Seetharama

AU - Moore, P. B.

AU - Richards, F. M.

PY - 1973/7/1

Y1 - 1973/7/1

N2 - 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.

AB - 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.

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JO - Biochemistry

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ER -

Cross-Linking of Elongation Factor EF-G to the 50S Ribosomal Subunit of Escherichia coli

Abstract

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