Functional aspects of ribosomal proteins.
A short personal recollection of HG Wittmann is given with emphasis on his basic contribution to the structure of the ribosome, in particular the ribosomal proteins. With these considerations in mind, two interrelated problems are reviewed here. The first relates to the internal symmetry both in tRNA and in the tetrameric L12-protein complex. The second problem to be addressed relates to the dynamics of transfer RNA in the ribosome and the role of L12 proteins in this process. The importance of electrostatic repulsion in the maintenance of the mutual spatial orientation of tRNAs and L12 in the ribosome is emphasized in relation to a pendulum model for how L12 may steer translocation.
Möller
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Department of Medical Biochemistry, Sylvius Laboratory, Faculty of Medicine, University of Leiden, The Netherlands.
D000595:Amino Acid Sequence; D006160:Guanosine Triphosphate / Q000378:metabolism; D008969:Molecular Sequence Data; D009426:Netherlands; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism
D010445:Peptide Elongation Factors; D012269:Ribosomal Proteins; C016700:ribosomal protein L7-L12; D006160:Guanosine Triphosphate; D012343:RNA, Transfer