Open AccessMethylation of elongation factor 1 alpha from the fungus Mucor.
Author(s) -
William R. Hiatt,
Roberto Garcia,
William C. Merrick,
Paul S. Sypherd
Publication year - 1982
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.79.11.3433
Subject(s) - elongation factor , mucor , hypha , biochemistry , biology , lysine , eukaryotic translation elongation factor 1 alpha 1 , yeast , fungus , elongation , fungal protein , alpha (finance) , microbiology and biotechnology , amino acid , saccharomyces cerevisiae , botany , rna , ribosome , aspergillus , gene , medicine , construct validity , materials science , nursing , ultimate tensile strength , patient satisfaction , metallurgy
A basic protein from the dimorphic fungus Mucor racemosus, found to be highly methylated, is shown to be protein synthesis elongation factor 1 alpha. This protein is the most abundant protein in hyphal cells but is less abundant in yeast cells. It is post-translationally methylated with the formation of mono-, di-, and trimethyllysine at as many as 16 sites. Nearly 20% of the 44 lysine residues of elongation factor 1 alpha from mycelia are modified while those from sporangiospores are virtually unmethylated.