Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system

被引:109
作者
Zitzewitz, JA
Ibarra-Molero, B
Fishel, DR
Terry, KL
Matthews, CR [1 ]
机构
[1] Penn State Univ, Dept Chem, Life Sci Consortium, University Pk, PA 16802 USA
[2] Penn State Univ, Dept Chem, Ctr Biomol Struct & Funct, University Pk, PA 16802 USA
关键词
protein folding; leucine zipper peptides; circular dichroism; helix formation; framework model;
D O I
10.1006/jmbi.2000.3507
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The structure of the transition state for the rate-limiting step in the folding and association of the homodimeric coiled-coil peptide GCN4-p1, was probed by mutational analysis. A series of quadruple amino acid replacements that spanned the helix propensity scale were made at the four external f positions in the heptad repeat. Equilibrium and kinetic circular dichroism studies demonstrate that both the stability and the unfolding and refolding rate constants vary with helix propensity but also reflect interactions of the altered side-chains with their local environments. Pairwise replacements and fragment studies show that the two C-terminal heptads are the likely source of the nucleating helices. Helix-helix recognition between preformed elements of secondary structure plays an important role in this fundamental folding reaction. (C) 2000 Academic Press.
引用
收藏
页码:1105 / 1116
页数:12
相关论文
共 47 条
  • [1] Amdur I., 1966, Chemical Kinetics: Principles and Selected Topics
  • [2] INTERACTIONS OF COILED COILS IN TRANSCRIPTION FACTORS - WHERE IS THE SPECIFICITY
    BAXEVANIS, AD
    VINSON, CR
    [J]. CURRENT OPINION IN GENETICS & DEVELOPMENT, 1993, 3 (02) : 278 - 285
  • [3] DESIGN OF 2-STRANDED AND 3-STRANDED COILED-COIL PEPTIDES
    BETZ, S
    FAIRMAN, R
    ONEIL, K
    LEAR, J
    DEGRADO, W
    [J]. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 1995, 348 (1323) : 81 - 88
  • [4] Bilsel O, 2000, ADV PROTEIN CHEM, V53, P153
  • [5] Chemical physics of protein folding
    Brooks, CL
    Gruebele, M
    Onuchic, JN
    Wolynes, PG
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (19) : 11037 - 11038
  • [6] Recognition between disordered states: Kinetics of the self-assembly of thioredoxin fragments
    Chaffotte, AF
    Li, JH
    Georgescu, RE
    Goldberg, ME
    Tasayco, ML
    [J]. BIOCHEMISTRY, 1997, 36 (51) : 16040 - 16048
  • [7] Chiti F, 1999, NAT STRUCT BIOL, V6, P380
  • [8] ALPHA-HELICAL COILED COILS - A WIDESPREAD MOTIF IN PROTEINS
    COHEN, C
    PARRY, DAD
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1986, 11 (06) : 245 - 248
  • [9] ALPHA-HELICAL COILED COILS AND BUNDLES - HOW TO DESIGN AN ALPHA-HELICAL PROTEIN
    COHEN, C
    PARRY, DAD
    [J]. PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1990, 7 (01): : 1 - 15
  • [10] THE PACKING OF ALPHA-HELICES - SIMPLE COILED-COILS
    CRICK, FHC
    [J]. ACTA CRYSTALLOGRAPHICA, 1953, 6 (8-9): : 689 - 697