Identification of a ribosomal protein essential for peptidyl transferase activity. | Zendy

Virginia G. Moore | Zendy; Robert E. Atchison | Zendy; George Thomas | Zendy; Michael F. Moran | Zendy; H F Noller | Zendy

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Identification of a ribosomal protein essential for peptidyl transferase activity.

Author(s) -

Virginia G. Moore,

Robert E. Atchison,

George Thomas,

Michael F. Moran,

H F Noller

Publication year - 1975

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.72.3.844

Subject(s) - peptidyl transferase , chemistry , transferase , lithium chloride , ribosomal protein , microbiology and biotechnology , biochemistry , enzyme , biology , ribosome , rna , organic chemistry , gene

Extraction with 2 M lithium chloride removes a group of proteins (LiC1 SP) from 50S ribosomal subunits. Both the LiC1 SP and the resulting cores, which contain the remaining proteins as well as 5S and 23S RNA, lack peptidyl transferase activity, as measured by the "fragment reaction". Activity can be restored to the LiC1 cores by reconstitution with LiC1 SP under conditions of high temperature and high ionic strength. The LiC1 SP proteins were fractionated by carboxymethyl-cellulose and Sephadex G-100, and the individual fractions were tested by this reconstitution system. Of the 18 ribosomal proteins found in the LiC1 SP, only L16 is essential for reconstitution of peptidyl transferase activity.

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