Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 16 March 1990:
Vol. 247. no. 4948, pp. 1306 - 1310
DOI: 10.1126/science.2315699

Articles

Science, Vol 247, Issue 4948, 1306-1310
Copyright © 1990 by American Association for the Advancement of Science


articles

Deciphering the message in protein sequences: tolerance to amino acid substitutions

JU Bowie, JF Reidhaar-Olson, WA Lim, and RT Sauer

Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

An amino acid sequence encodes a message that determines the shape and function of a protein. This message is highly degenerate in that many different sequences can code for proteins with essentially the same structure and activity. Comparison of different sequences with similar messages can reveal key features of the code and improve understanding of how a protein folds and how it performs its function.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
In Planta Mutagenesis Determines the Functional Regions of the Wheat Puroindoline Proteins.
L. Feiz, B. S. Beecher, J. M. Martin, and M. J. Giroux (2009)
Genetics 183, 853-860
   Abstract »    Full Text »    PDF »
Structural imperatives impose diverse evolutionary constraints on helical membrane proteins.
A. Oberai, N. H. Joh, F. K. Pettit, and J. U. Bowie (2009)
PNAS 106, 17747-17750
   Abstract »    Full Text »    PDF »
Crystal structure of an extensively simplified variant of bovine pancreatic trypsin inhibitor in which over one-third of the residues are alanines.
M. M. Islam, S. Sohya, K. Noguchi, M. Yohda, and Y. Kuroda (2008)
PNAS 105, 15334-15339
   Abstract »    Full Text »    PDF »
Template properties of mutagenic cytosine analogues in reverse transcription.
T. Suzuki, K. Moriyama, C. Otsuka, D. Loakes, and K. Negishi (2006)
Nucleic Acids Res. 34, 6438-6449
   Abstract »    Full Text »    PDF »
Direct evolution of genetic robustness in microRNA.
E. Borenstein and E. Ruppin (2006)
PNAS 103, 6593-6598
   Abstract »    Full Text »    PDF »
Regulation of Sexual Dimorphism: Mutational and Chemogenetic Analysis of the Doublesex DM Domain.
W. Zhang, B. Li, R. Singh, U. Narendra, L. Zhu, and M. A. Weiss (2006)
Mol. Cell. Biol. 26, 535-547
   Abstract »    Full Text »    PDF »
Progress in Modeling of Protein Structures and Interactions.
O. Schueler-Furman, C. Wang, P. Bradley, K. Misura, and D. Baker (2005)
Science 310, 638-642
   Abstract »    Full Text »    PDF »
Protein Structural Influences in Rhodopsin Evolution.
L. Marsh and C. S. Griffiths (2005)
Mol. Biol. Evol. 22, 894-904
   Abstract »    Full Text »    PDF »
Consolidating critical binding determinants by noncyclic rearrangement of protein secondary structure.
R. K. Tabtiang, B. O. Cezairliyan, R. A. Grant, J. C. Cochrane, and R. T. Sauer (2005)
PNAS 102, 2305-2309
   Abstract »    Full Text »    PDF »
Protein tolerance to random amino acid change.
H. H. Guo, J. Choe, and L. A. Loeb (2004)
PNAS 101, 9205-9210
   Abstract »    Full Text »    PDF »
Identification of conserved residue patterns in small {beta}-barrel proteins.
R. Qamra, B. Taneja, and S. C. Mande (2002)
Protein Eng. Des. Sel. 15, 967-977
   Abstract »    Full Text »    PDF »
Combinatorial mutagenesis to restrict amino acid usage in an enzyme to a reduced set.
S. Akanuma, T. Kigawa, and S. Yokoyama (2002)
PNAS 99, 13549-13553
   Abstract »    Full Text »    PDF »
Domain Architecture of a High Mobility Group A-type Bacterial Transcriptional Factor.
S. Padmanabhan, M. Elias-Arnanz, E. Carpio, P. Aparicio, and F. J. Murillo (2001)
J. Biol. Chem. 276, 41566-41575
   Abstract »    Full Text »    PDF »
Minor structural consequences of alternative CUG codon usage (Ser for Leu) in Candida albicans exoglucanase.
J.F. Cutfield, P.A. Sullivan, and S.M. Cutfield (2000)
Protein Eng. Des. Sel. 13, 735-738
   Abstract »    Full Text »    PDF »
Monomeric Structure of the Human EphB2 Sterile alpha Motif Domain.
C. D. Thanos, S. Faham, K. E. Goodwill, D. Cascio, M. Phillips, and J. U. Bowie (1999)
J. Biol. Chem. 274, 37301-37306
   Abstract »    Full Text »    PDF »
Effects of F171 Mutations in the 6'-N-Acetyltransferase Type Ib [AAC(6')-Ib] Enzyme on Susceptibility to Aminoglycosides.
R. Chavideh, S. Sholly, D. Panaite, and M. E. Tolmasky (1999)
Antimicrob. Agents Chemother. 43, 2811-2812
   Abstract »    Full Text »
Conformation and stability of barley chymotrypsin inhibitor-2 (CI-2) mutants containing multiple lysine substitutions.
K. R. Roesler and A. G. Rao (1999)
Protein Eng. Des. Sel. 12, 967-973
   Abstract »    Full Text »    PDF »
Analysis of Thermal Stabilizing Interactions in Mesophilic and Thermophilic Adenylate Kinases from the Genus Methanococcus.
P. J. Haney, M. Stees, and J. Konisky (1999)
J. Biol. Chem. 274, 28453-28458
   Abstract »    Full Text »    PDF »
Modeling evolutionary landscapes: Mutational stability, topology, and superfunnels in sequence space.
E. Bornberg-Bauer and H. S. Chan (1999)
PNAS 96, 10689-10694
   Abstract »    Full Text »    PDF »
Susceptibility of {beta}-lactamase to core amino acid substitutions.
J. F. Petrosino, M. Baker, and T. Palzkill (1999)
Protein Eng. Des. Sel. 12, 761-769
   Abstract »    Full Text »    PDF »
Single Amino Acid Substitutions Globally Suppress the Folding Defects of Temperature-sensitive Folding Mutants of Phage P22 Coat Protein.
L. A. Aramli and C. M. Teschke (1999)
J. Biol. Chem. 274, 22217-22224
   Abstract »    Full Text »    PDF »
Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species.
P. J. Haney, J. H. Badger, G. L. Buldak, C. I. Reich, C. R. Woese, and G. J. Olsen (1999)
PNAS 96, 3578-3583
   Abstract »    Full Text »    PDF »
Tolerance of Arc repressor to multiple-alanine substitutions.
B. M. Brown and R. T. Sauer (1999)
PNAS 96, 1983-1988
   Abstract »    Full Text »    PDF »
Compensatory Changes in GroEL/Gp31 Affinity as a Mechanism for Allele-specific Genetic Interaction.
A. Richardson, S. M. van der Vies, F. Keppel, A. Taher, S. J. Landry, and C. Georgopoulos (1999)
J. Biol. Chem. 274, 52-58
   Abstract »    Full Text »    PDF »
Novel Allergen Structures with Tandem Amino Acid Repeats Derived from German and American Cockroach.
A. Pomes, E. Melen, L. D. Vailes, J. D. Retief, L. K. Arruda, and M. D. Chapman (1998)
J. Biol. Chem. 273, 30801-30807
   Abstract »    Full Text »    PDF »
Hydrophobic sequence minimization of the alpha -lactalbumin molten globule.
L. C. Wu and P. S. Kim (1997)
PNAS 94, 14314-14319
   Abstract »    Full Text »    PDF »
De Novo Protein Design: Fully Automated Sequence Selection.
B. I. Dahiyat and S. L. Mayo (1997)
Science 278, 82-87
   Abstract »    Full Text »
A natural polymorphism in beta -lactamase is a global suppressor.
W. Huang and T. Palzkill (1997)
PNAS 94, 8801-8806
   Abstract »    Full Text »    PDF »
Functional Requirements for Inhibition of Thrombin by Antithrombin III in the Presence and Absence of Heparin.
M. Tsiang, A. K. Jain, and C. S. Gibbs (1997)
J. Biol. Chem. 272, 12024-12029
   Abstract »    Full Text »    PDF »
Protein Design: The Choice of de Novo Sequences.
J. R. Beasley and M. H. Hecht (1997)
J. Biol. Chem. 272, 2031-2034
   Full Text »    PDF »
Tolerance to Amino Acid Variations in Peptides Binding to the Major Histocompatibility Complex Class I Protein H-2K^b.
K. Udaka, K.-H. Wiesmüller, S. Kienle, Gün. Jung, and P. Walden (1995)
J. Biol. Chem. 270, 24130-24134
   Abstract »    Full Text »    PDF »
Saturation Mutagenesis of Human Interleukin-3.
P. O. Olins, S. C. Bauer, S. Braford-Goldberg, K. Sterbenz, J. O. Polazzi, M. H. Caparon, B. K. Klein, A. M. Easton, K. Paik, J. A. Klover, et al. (1995)
J. Biol. Chem. 270, 23754-23760
   Abstract »    Full Text »    PDF »
Functional Mapping of the Surface Residues of Human Thrombin.
M. Tsiang, A. K. Jain, K. E. Dunn, M. E. Rojas, L. L. K. Leung, and C. S. Gibbs (1995)
J. Biol. Chem. 270, 16854-16863
   Abstract »    Full Text »    PDF »
Protein design by binary patterning of polar and nonpolar amino acids.
S Kamtekar, J. Schiffer, H Xiong, J. Babik, and M. Hecht (1993)
Science 262, 1680-1685
   Abstract »    PDF »
Colicin E1 binding to membranes: time-resolved studies of spin-labeled mutants.
Y. Shin, C Levinthal, F Levinthal, and W. Hubbell (1993)
Science 259, 960-963
   Abstract »
A method to identify protein sequences that fold into a known three-dimensional structure.
J. Bowie, R Luthy, and D Eisenberg (1991)
Science 253, 164-170
   Abstract »    PDF »
Global suppression of protein folding defects and inclusion body formation.
A Mitraki, B Fane, C Haase-Pettingell, J Sturtevant, and J King (1991)
Science 253, 54-58
   Abstract »    PDF »
A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids.
K. O'Neil and W. DeGrado (1990)
Science 250, 646-651
   Abstract »    PDF »
An insertion in the human thyrotropin receptor critical for high affinity hormone binding.
H. Wadsworth, G. Chazenbalk, Y Nagayama, D Russo, and B Rapoport (1990)
Science 249, 1423-1425
   Abstract »    PDF »
Assignment of Functional Amino Acids around the Active Site of Human DNA Topoisomerase IIalpha.
Y. Okada, Y. Ito, A. Kikuchi, Y. Nimura, S. Yoshida, and M. Suzuki (2000)
J. Biol. Chem. 275, 24630-24638
   Abstract »    Full Text »    PDF »
Regulation of the Cystic Fibrosis Transmembrane Conductance Regulator Cl- Channel by Its R Domain.
L. S. Ostedgaard, O. Baldursson, and M. J. Welsh (2001)
J. Biol. Chem. 276, 7689-7692
   Full Text »    PDF »
A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution.
L. S. Ostedgaard, O. Baldursson, D. W. Vermeer, M. J. Welsh, and A. D. Robertson (2000)
PNAS 97, 5657-5662
   Abstract »    Full Text »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)