145 research outputs found
Protein phosphorylation in yeast mitochondria
We describe the identification and submitochondrial localization of four protein kinases and of their target proteins in derepressed yeast mitochondria. The activity of one of the kinases depends on the presence of cyclic AMP (cAMP). It is soluble and localized in the mitochondrial intermembrane space. Its natural target is a polypeptide of 40 kDa molecular mass, which is bound to the inner membrane. Besides this natural target this kinase phosphorylates acidic heterologous proteins, like casein, with high efficiency. The other protein kinases identified so far are cAMP-independent. At least one is localized in the matrix having its natural substrates (49 and 24 kDa) in the same compartment. Two others are firmly bound to the inner membrane phosphorylating target proteins in the inner membrane (52·5 kDa) and in the intermembrane space (17·5 kDa), respectively
Functional dichotomy of ribosomal proteins during the synthesis of mammalian 40S ribosomal subunits
Subsets of 40S ribosomal subunits are required for initiating rRNA processing, rRNA maturation, and nuclear export
Preferential Utilization of Phosphorylated 40-S Ribosomal Subunits during Initiation Complex Formation
RIBOSOMAL PROTEIN PHOSPHORYLATION AND CONTROL OF CELL GROWTH11This work was supported by NIH grant CA 22250 and grant IN103-C frcm the American Cancer Society.
Phosphorylation of Ribosomal Protein S6. Relationship to Protein Synthesis in HeLa Cells
The Phosphorylation of Ribosomal Protein S6 from Progesterone-Stimulated Xenopus laevis Oocytes
Regulation of ribosome phosphorylation and antibiotic sensitivity in tetrahymena thermophila: A correlation
Rapid Alterations in Initiation Rate and Recruitment of Inactive RNA Are Temporally Correlated with S6 Phosphorylation
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