The primary structure of protein L9 from the Escherichia coli ribosome

FEBS Letters

Kamp, Roza Maria¹  Wittmann-Liebold, Brigitte¹ 

[1] Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, D-1000 Berlin 33 (Dahlem), Germany

关键词: E. coli ribosome;    Large subunit protein L9;    Primary structure determination;    Secondary structure prediction;    Homologies to other ribosomal proteins;   

DOI  :  10.1016/0014-5793(82)81123-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The primary structure of protein L9 from the large subunit of the E. coli ribosome has completely been determined. Automatic sequencing of the intact protein by means of an improved Beckman sequencer and by manual sequencing of diverse peptides deriving from cleavages with trypsin, thermolysin, chymotrypsin and pepsin by the DABITC/PITC double coupling method [FEBS Lett. (1978) 93, 205–214] have been performed to establish the amino acid sequence. Protein L9 contains 148 amino acid residues and has a molecular mass of 15 696. Predictions of secondary structural elements for this protein have been made. A strong homology exists between the primary structure of the E. coli protein L9 and a B. stearothermophilus ribosomal protein previously crystallized [FEBS Lett. (1979) 103, 66–70].

【 授权许可】

Unknown