Macromolecular mimicry

Some proteins have been shown to mimic the overall shape and structure of nucleic acids. For some of the proteins involved in translating the genetic information into proteins on the ribosome particle, there are indications that such observations of macromolecular mimicry even extend to similarity in interaction with and function on the ribosome. A small number of structural results obtained outside the protein biosynthesis machinery could indicate that the concept of macromolecular mimicry between proteins and nucleic acids is more general. The implications for the function and evolution of protein biosynthesis are discussed.

[1]  N. Seeman,et al.  Sequence-specific Recognition of Double Helical Nucleic Acids by Proteins (base Pairs/hydrogen Bonding/recognition Fidelity/ion Binding) , 2022 .

[2]  Harry F. Noller,et al.  Intermediate states in the movement of transfer RNA in the ribosome , 1989, Nature.

[3]  A. Oldstone Molecular Mimicry , 1989, Current Topics in Microbiology and Immunology.

[4]  N. Pavletich,et al.  Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A , 1991, Science.

[5]  P. Kraulis A program to produce both detailed and schematic plots of protein structures , 1991 .

[6]  R. Hilgenfeld,et al.  Crystal structure of active elongation factor Tu reveals major domain rearrangements , 1993, Nature.

[7]  John W. R. Schwabe,et al.  The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition , 1993, Nature.

[8]  Steven Hahn,et al.  Crystal structure of a yeast TBP/TATA-box complex , 1993, Nature.

[9]  J. Nyborg,et al.  The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. , 1993, Structure.

[10]  E A Merritt,et al.  Raster3D Version 2.0. A program for photorealistic molecular graphics. , 1994, Acta crystallographica. Section D, Biological crystallography.

[11]  A. Liljas,et al.  Three‐dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. , 1994, The EMBO journal.

[12]  Stephen K. Burley,et al.  1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG , 1994, Nature Structural Biology.

[13]  T. Steitz,et al.  The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. , 1994, The EMBO journal.

[14]  J. Frank,et al.  A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome , 1995, Nature.

[15]  J. Doudna,et al.  Selection of an RNA molecule that mimics a major autoantigenic epitope of human insulin receptor. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[16]  David A. Case,et al.  Structural basis for DNA bending by the architectural transcription factor LEF-1 , 1995, Nature.

[17]  J. Tainer,et al.  Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: Protein mimicry of DNA , 1995, Cell.

[18]  M van Heel,et al.  The 70S Escherichia coli ribosome at 23 A resolution: fitting the ribosomal RNA. , 1995, Structure.

[19]  S Thirup,et al.  Crystal Structure of the Ternary Complex of Phe-tRNAPhe, EF-Tu, and a GTP Analog , 1995, Science.

[20]  C. Kundrot,et al.  Crystal Structure of a Group I Ribozyme Domain: Principles of RNA Packing , 1996, Science.

[21]  A. Liljas Protein synthesis: Imprinting through molecular mimicry , 1996, Current Biology.

[22]  Michael Wulff,et al.  The structure of the Escherichia coli EF-Tu· EF-Ts complex at 2.5 Å resolution , 1996, Nature.

[23]  A. Liljas,et al.  The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. , 1996, Structure.

[24]  J. Nyborg,et al.  The GTP binding motif: variations on a theme , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[25]  Rolf Hilgenfeld,et al.  An α to β conformational switch in EF-Tu , 1996 .

[26]  J. Nyborg,et al.  Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation. , 1996, Trends in biochemical sciences.

[27]  E. Kandel,et al.  Control of Memory Formation Through Regulated Expression of a CaMKII Transgene , 1996, Science.

[28]  J. Keene RNA surfaces as functional mimetics of proteins. , 1996, Chemistry & biology.

[29]  A. Kaji,et al.  Dual functions of ribosome recycling factor in protein biosynthesis: disassembling the termination complex and preventing translational errors. , 1996, Biochimie.

[30]  Y. Nakamura,et al.  Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[31]  G. Varani,et al.  Solution structure of the N-terminal RNP domain of U1A protein: the role of C-terminal residues in structure stability and RNA binding. , 1996, Journal of molecular biology.

[32]  S Thirup,et al.  Helix unwinding in the effector region of elongation factor EF-Tu-GDP. , 1996, Structure.

[33]  J. Frank,et al.  Direct Visualization of A-, P-, and E-Site Transfer RNAs in the Escherichia coli Ribosome , 1996, Science.

[34]  C. Oubridge,et al.  Two structurally different RNA molecules are bound by the spliceosomal protein U1A using the same recognition strategy. , 1996, Structure.

[35]  F. Jurnak,et al.  A complex profile of protein elongation: translating chemical energy into molecular movement. , 1996, Structure.

[36]  R. Brimacombe,et al.  Visualization of elongation factor Tu on the Escherichia coli ribosome , 1997, Nature.

[37]  R. Buckingham,et al.  Polypeptide chain release factors , 1997, Molecular microbiology.

[38]  J. Davies Molecular mimicry: Can epitope mimicry induce autoimmune disease? , 1997, Immunology and cell biology.

[39]  P. Sigler,et al.  Crystal structure of the EF-Tu˙EF-Ts complex from Thermus thermophilus , 1997, Nature Structural Biology.

[40]  R. Brimacombe,et al.  Arrangement of tRNAs in Pre- and Posttranslocational Ribosomes Revealed by Electron Cryomicroscopy , 1997, Cell.

[41]  L. Kisselev,et al.  Eukaryotic release factor 1 (eRF1) abolishes readthrough and competes with suppressor tRNAs at all three termination codons in messenger RNA. , 1997, Nucleic acids research.

[42]  M. Ehrenberg,et al.  A direct estimation of the context effect on the efficiency of termination. , 1998, Journal of molecular biology.

[43]  J Frank,et al.  Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[44]  A. Kaji,et al.  Disassembly of the post-termination complex and reduction of translational error by ribosome recycling factor (RRF)-A possible new target for antibacterial agents. , 1998, Biochemical and biophysical research communications.

[45]  S. Mottagui-Tabar,et al.  Evidence for in vivo ribosome recycling, the fourth step in protein biosynthesis , 1998, The EMBO journal.

[46]  RNA Mimicry in the Translational Apparatus , 1998 .

[47]  L. Kay,et al.  Solution Structure of a TBP–TAFII230 Complex Protein Mimicry of the Minor Groove Surface of the TATA Box Unwound by TBP , 1998, Cell.

[48]  R. Giegé,et al.  tRNA mimics. , 1998, Current opinion in structural biology.

[49]  S. Harrison,et al.  Differing roles for zinc fingers in DNA recognition: structure of a six-finger transcription factor IIIA complex. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[50]  S. Cusack,et al.  tRNA(Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase. , 1998, Structure.

[51]  G. Blobel,et al.  Crystallographic Analysis of the Recognition of a Nuclear Localization Signal by the Nuclear Import Factor Karyopherin α , 1998, Cell.

[52]  R. Hilgenfeld,et al.  Structure and expression of elongation factor Tu from Bacillus stearothermophilus. , 1998, Journal of molecular biology.

[53]  B. Clark,et al.  Macromolecular Mimicry of Nucleic Acid and Protein , 1999, IUBMB life.

[54]  M. R. Parsons,et al.  Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution. , 1999, Journal of molecular biology.

[55]  M. Selmer,et al.  Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic. , 1999, Science.

[56]  M. Ehrenberg,et al.  Novel roles for classical factors at the interface between translation termination and initiation. , 1999, Molecular cell.

[57]  T. Earnest,et al.  X-ray crystal structures of 70S ribosome functional complexes. , 1999, Science.

[58]  V. Ramakrishnan,et al.  Structure of a bacterial 30S ribosomal subunit at 5.5 Å resolution , 1999, Nature.

[59]  Poul Nissen,et al.  Placement of protein and RNA structures into a 5 Å-resolution map of the 50S ribosomal subunit , 1999, Nature.

[60]  W. Whelan A Welcome to IUBMB Life , 1999 .

[61]  S Thirup,et al.  The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. , 1999, Structure.

[62]  V. Ramakrishnan,et al.  The structure of a bacterial 30S ribosomal subunit , 2000 .