The yeast 5S rRNA binding ribosomal protein YL3 is phosphorylated in vivo.
The 5S rRNA-ribosomal protein YL3 ribonucleoprotein particle was isolated from yeast cells labeled with [32P]orthophosphate. The protein moiety was purified and found to be radioactive. Labeled phosphoserine was detected after partial hydrolysis of the protein. Up to two phosphate residues are sterified per mole of YL3 ribosomal protein.
Campos
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F
Departamento de Genética y Biología Molecular, Centro de Investigacíon y de Estudios Avanzados del I.P.N., Mexico City, Mexico.
Corona-Reyes
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M
Zinker
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S
D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000378:metabolism*; D010766:Phosphorylation; D010768:Phosphoserine / Q000032:analysis; D012341:RNA, Ribosomal, 5S / Q000378:metabolism*; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins
D005656:Fungal Proteins; D012341:RNA, Ribosomal, 5S; D016601:RNA-Binding Proteins; C489268:RPL5 protein, S cerevisiae; D012269:Ribosomal Proteins; D029701:Saccharomyces cerevisiae Proteins; D010768:Phosphoserine