Crystallization and Structural Studies of Ribosomal Proteins from Thermus thermophilus and Methanococcus jannaschii
Maria GARBER*a, Natalia DAVYDOVa, George GONGADZEa, Roman FEDOROVa, Alfia KHAIRULLINAa, Vladimir MESHCHERYAKOVa, Natalia NEVSKAYAa, Stanislav NIKONOVa, Alexei NIKULINa, Svetlana TISHCHENKOa, Bernard EHRESMANNb, Anders LILJASc, and Wolfgang PIENDLd
a Institute of Protein Research, 142292 Pushchino, Moscow Region RUSSIA
b Institute de Biologie Moleculaire et Cellulaire, Strasbourg, FRANCE
c Chemical Center, University of Lund, PO Box 124, S-221 00, Lund, SWEDEN
e Institute fur Med. Chemie und Biochemie, Universitat Innsbruck, A-6020 Innsbruck, AUSTRIA
Ribosomes from different kingdoms contain from 50 to over 80 distinct ribosomal proteins. Some of these proteins are conserved in all types of ribosomes. Current structural studies are focused on ribosomal proteins from thermophilic bacteria (Bacillus stearothermophilus and Thermus therrnophilus) which have been overproduced in E. coli. The structures of fourteen ribosomal proteins have been solved: S5, S6, S7, S8, S15, S17, L1, L6, L9, L11, L12, L14, L22, L30. The structures of S8 and L30 have been solved from both Bst and Tth. Comparison of homological protein structures from the extreme and moderate thermophiles have been done and important similarities as well as differences have been found.
Archaeal proteins share structural features with bacterial as well as with eukaryotic homologs. Moreover archaeal proteins are more closely related to eukaryotic counterparts. No structures of archaeal ribosomal proteins have been determined so far. Recently we have succeeded in crystallization of ribosomal protein L1 from hyperthermophilic Archaeon Methanococcusjannaschii. Crystals diffract to at least 2.5Å, resolution and belong to the space group P1 with parameters of crystal unit a=34.40Å, b=40.23Å, c=56.35Å, α=83.41, β=80.66, γ=75.06. This result offers a possibility to determine the first structure of an archaeal ribosomal protein. Earlier we solved the structure of TthL 1. Comparison of structures of two homological ribosomal proteins from different kingdoms will provide very important information on the evolution of ribosomal proteins and on the organization of their RNA-binding sites.
