Isolation, characterization, phosphorylation and site of synthesis ofSpinaciachloroplast ribosomal proteins

✍ Scribed by Mark Posno; Marjolein Noort; Roger Débise; Gert S. P. Groot

• Book ID: 104768502
• Publisher: Springer-Verlag
• Year: 1984
• Tongue: English
• Weight: 466 KB
• Volume: 8
• Category: Article
• ISSN: 0172-8083
• DOI: 10.1007/bf00420227

✦ Synopsis

We have characterized the ribosomal proteins from Spinacia chloroplasts using two-dimensional gel electrophoresis. The 30S and 50S subunits contain 23-25 and 36 ribosomal proteins, respectively. In contrast to prokaryotic ribosomes, chloroplast ribosomes contain at least one (and possibly two) phosphorylated ribosomal proteins. Isolated chloroplasts synthesize in the presence of ((35)S) labeled methionine and cysteine at least seven 30S and thirteen 50S ribosomal proteins which are assembled into (pre)ribosomes. This suggests that about one third of the chloroplast ribosomal proteins is encoded by the chloroplast DNA itself. The identity of several labeled proteins in the two-dimensional gel electrophoretic patterns which did not comigrate with stained chloroplast ribosomal proteins is discussed.