Evidence for regulation of protein synthesis at the elongation step by CDK1/cyclin B phosphorylation | Zendy

Annabelle Monnier | Zendy

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Evidence for regulation of protein synthesis at the elongation step by CDK1/cyclin B phosphorylation

Author(s) -

Annabelle Monnier

Publication year - 2001

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/29.7.1453

Subject(s) - elongation factor , cyclin dependent kinase 1 , biology , ef tu , elongation , biochemistry , protein biosynthesis , phosphorylation , phenylalanine , cyclin b , serine , cyclin a , microbiology and biotechnology , cell cycle , cyclin , transfer rna , amino acid , rna , cell , ribosome , materials science , ultimate tensile strength , gene , metallurgy

Eukaryotic elongation factor 1 (eEF-1) contains the guanine nucleotide exchange factor eEF-1B that loads the G protein eEF-1A with GTP after each cycle of elongation during protein synthesis. Two features of eEF-1B have not yet been elucidated: (i) the presence of the unique valyl-tRNA synthetase; (ii) the significance of target sites for the cell cycle protein kinase CDK1/cyclin B. The roles of these two features were addressed by elongation measurements in vitro using cell-free extracts. A poly(GUA) template RNA was generated to support both poly(valine) and poly(serine) synthesis and poly(phenylalanine) synthesis was driven by a poly(uridylic acid) template. Elongation rates were in the order phenylalanine > valine > serine. Addition of CDK1/cyclin B decreased the elongation rate for valine whereas the rate for serine and phenylalanine elongation was increased. This effect was correlated with phosphorylation of the eEF-1delta and eEF-1gamma subunits of eEF-1B. Our results demonstrate specific regulation of elongation by CDK1/cyclin B phosphorylation.

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