Affinity labelling the acceptor site of the peptidyl transferase centre of the Escherichia coli ribosome

Dan Eilat; Maria Pellegrini; Helen Oen; Nathan De Groot; Yehuda Lapidot; Charles R. Cantor

doi:10.1038/250514a0

Affinity labelling the acceptor site of the peptidyl transferase centre of the Escherichia coli ribosome

Dan Eilat
, Maria Pellegrini^*
, Helen Oen
, Nathan De Groot
, Yehuda Lapidot
, Charles R. Cantor

^*Corresponding author for this work

Alexander Silberman Institute of Life Sciences

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

25 Scopus citations

Abstract

WE have identified two 50S proteins, L2 and L26-L27, in the peptidyl (P) site of the peptidyl transferase centre of E. coli ribosomes¹ BrAc-³H-Phe-tRNA^phe, a peptidyl-tRNA affinity analogue, was shown to bind specifically to the P site and covalently react with only L2 and L26-L27. The ability of the same molecules of ribosome-bound BrAcPhe-tRNA^phe to participate in dipeptide formation and covalent attachment to ribosomal proteins was the most compelling evidence for functional P site binding.

Original language	English
Pages (from-to)	514-516
Number of pages	3
Journal	Nature
Volume	250
Issue number	5466
DOIs	https://doi.org/10.1038/250514a0
State	Published - 1974

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title = "Affinity labelling the acceptor site of the peptidyl transferase centre of the Escherichia coli ribosome",

abstract = "WE have identified two 50S proteins, L2 and L26-L27, in the peptidyl (P) site of the peptidyl transferase centre of E. coli ribosomes1 BrAc-3H-Phe-tRNAphe, a peptidyl-tRNA affinity analogue, was shown to bind specifically to the P site and covalently react with only L2 and L26-L27. The ability of the same molecules of ribosome-bound BrAcPhe-tRNAphe to participate in dipeptide formation and covalent attachment to ribosomal proteins was the most compelling evidence for functional P site binding.",

author = "Dan Eilat and Maria Pellegrini and Helen Oen and \{De Groot\}, Nathan and Yehuda Lapidot and Cantor, \{Charles R.\}",

year = "1974",

doi = "10.1038/250514a0",

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AU - Eilat, Dan

AU - Pellegrini, Maria

AU - Oen, Helen

AU - De Groot, Nathan

AU - Lapidot, Yehuda

AU - Cantor, Charles R.

PY - 1974

Y1 - 1974

N2 - WE have identified two 50S proteins, L2 and L26-L27, in the peptidyl (P) site of the peptidyl transferase centre of E. coli ribosomes1 BrAc-3H-Phe-tRNAphe, a peptidyl-tRNA affinity analogue, was shown to bind specifically to the P site and covalently react with only L2 and L26-L27. The ability of the same molecules of ribosome-bound BrAcPhe-tRNAphe to participate in dipeptide formation and covalent attachment to ribosomal proteins was the most compelling evidence for functional P site binding.

AB - WE have identified two 50S proteins, L2 and L26-L27, in the peptidyl (P) site of the peptidyl transferase centre of E. coli ribosomes1 BrAc-3H-Phe-tRNAphe, a peptidyl-tRNA affinity analogue, was shown to bind specifically to the P site and covalently react with only L2 and L26-L27. The ability of the same molecules of ribosome-bound BrAcPhe-tRNAphe to participate in dipeptide formation and covalent attachment to ribosomal proteins was the most compelling evidence for functional P site binding.

UR - https://www.scopus.com/pages/publications/0016354121

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DO - 10.1038/250514a0

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SP - 514

EP - 516

JO - Nature

JF - Nature

IS - 5466

ER -

Affinity labelling the acceptor site of the peptidyl transferase centre of the Escherichia coli ribosome

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