Localization of the protein L2 in the 50 S subunit and the 70 S E. coli ribosome

• Published in: Journal of molecular biology Vol. 305; no. 1; pp. 167 - 177
• Main Authors: Willumeit, Regine, Forthmann, Stefan, Beckmann, Jörn, Diedrich, Gundo, Ratering, Ralf, Stuhrmann, Heinrich B, Nierhaus, Knud H
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 05.01.2001
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Binding Sites; Electrophoresis, Gel, Two-Dimensional; Escherichia coli; Escherichia coli - chemistry; Escherichia coli - genetics; Models, Molecular; neutron scattering; Neutrons; protein biosynthesis; Protein Structure, Quaternary; Protein Subunits; Protons; ribosomal protein L2; Ribosomal Proteins - chemistry; Ribosomal Proteins - metabolism; ribosomal subunit 30S; ribosomal subunit 50S; Ribosomes - chemistry; Ribosomes - genetics; Ribosomes - metabolism; RNA, Bacterial - metabolism; RNA, Ribosomal - metabolism; Scattering, Radiation; spin-contrast variation; neutron scattering; spin-contrast variation; protein biosynthesis; ribosomal protein L2
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1006/jmbi.2000.4289

The protein L2 is found in all ribosomes and is one of the best conserved proteins of this mega-dalton complex. The protein was localized within both the isolated 50 S subunit and the 70 S ribosome of the Escherichia coli bacteria with the neutron-scattering technique of spin-contrast variation. L2 is elongated, exposing one end of the protein to the surface of the intersubunit interface of the 50 S subunit. The protein changes its conformation slightly when the 50 S subunit reassociates with the 30 S subunit to form a 70 S ribosome, becoming more elongated and moving approximately 30 Å into the 50 S matrix. The results support a recent observation that L2 is essential for the association of the ribosomal subunits and might participate in the binding and translocation of the tRNAs.