Open AccessProtein phosphorylation in the Archaebacterium Sulfolobus acidocaldarius
Author(s) -
SKÓRKO Romuald
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08601.x
Subject(s) - sulfolobus acidocaldarius , phosphorylation , threonine , serine , biochemistry , biology , protein phosphorylation , phosphoserine , ribosomal protein , rna polymerase , rna , archaea , gene , ribosome , protein kinase a
A number of proteins of the sulphur‐dependent archaebacterium Sulfolobus acidocaldarius are phosphorylated in vivo . The extent of phosphorylation depends on the state of growth and is most intense in the late exponential phase. Some of the phosphorylated proteins are strongly associated with the bacterial membrane. Ribosomal proteins and DNA‐dependent RNA polymerase are not phosphorylated. Studies in vitro show a high target selectivity. The activity is not increased by cyclic nucleotides. The reaction in vitro is optimal in the presence of Mg 2+ , Mn 2+ or Ca 2+ . Both serine and threonine residues are modified. Acetate ions do not induce additional phosphorylation.