On the structure of the scaffolding core of bacteriophage T4

被引:2
|
作者
Berger, B [1 ]
Hoest, GW
Paulson, JR
Shor, PW
机构
[1] MIT, Dept Math, Cambridge, MA 02139 USA
[2] MIT, Comp Sci Lab, Cambridge, MA 02139 USA
[3] Univ Wisconsin, Dept Chem, Oshkosh, WI 54901 USA
[4] AT&T Bell Labs, Florham Park, NJ USA
关键词
bacteriophage T4; electron microscopy; scaffolding proteins; self-assembly;
D O I
10.1089/cmb.1999.6.1
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The scaffolding core in bacteriophages is a temporary structure that plays a major role in determining the shape of the protein shell that encapsulates the viral DNA, In the currently accepted structure for the scaffolding core in bacteriophage T4, there is a symmetry mismatch between the protein shell, which has fivefold symmetry, and the scaffolding core, which is believed to consist of six helical chains, The analysis of T4 giant prohead data that was used to determine this structure made an implicit assumption about the manner in which giant proheads flatten during preparation for electron microscopy, Namely, it was assumed that techniques for analysis of Fourier transforms of flattened single-layer cylinders could be applied independently to the shell and the core. This analysis makes the implicit assumption that connections between the core and the shell do not affect the flattening process, and thus are stretched or broken during the flattening process. Reexamination of the experimental data shows that this assumption is likely to be incorrect. A reanalysis shows that the data could be consistent with six, eight, or 10 helical chains, and is a better match for eight or 10 helical chains. Ten helical chains would match the fivefold symmetry of the shell. The 10-helix core model is particularly attractive because it suggests st Vernier mechanism, which is able to explain the process of length determination in giant head mutants of T4, It is possible that the same assumption has been made for structural analysis of other biological systems. If this is the case, any results obtained should also be reexamined.
引用
收藏
页码:1 / 12
页数:12
相关论文
共 50 条
  • [21] The crystal structure of the UvsW helicase from bacteriophage T4
    Sickmier, EA
    Kreuzer, KN
    White, SW
    STRUCTURE, 2004, 12 (04) : 583 - 592
  • [22] The tail structure of bacteriophage T4 and its mechanism of contraction
    Kostyuchenko, VA
    Chipman, PR
    Leiman, PG
    Arisaka, F
    Mesyanzhinov, VV
    Rossmann, MG
    NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2005, 12 (09) : 810 - 813
  • [23] Structure of the cell-puncturing device of bacteriophage T4
    Kanamaru, S
    Leiman, PG
    Kostyuchenko, VA
    Chipman, PR
    Mesyanzhinov, VV
    Arisaka, F
    Rossmann, MG
    NATURE, 2002, 415 (6871) : 553 - 557
  • [24] STRUCTURE OF NORMAL AND CONTRACTED TAIL SHEATHS OF T4 BACTERIOPHAGE
    KRIMM, S
    ANDERSON, TF
    JOURNAL OF MOLECULAR BIOLOGY, 1967, 27 (02) : 197 - &
  • [25] Structure, Assembly, and DNA Packaging of the Bacteriophage T4 Head
    Black, Lindsay W.
    Rao, Venigalla B.
    ADVANCES IN VIRUS RESEARCH, VOL 82: BACTERIOPHAGES, PT A, 2012, 82 : 119 - 153
  • [26] Investigation of the oligomeric structure of the bacteriophage T4 Dda helicase
    Laurent, RS
    Babb, KB
    Morris, PD
    Raney, KD
    FASEB JOURNAL, 1997, 11 (09): : A1371 - A1371
  • [27] Structure of the cell-puncturing device of bacteriophage T4
    Shuji Kanamaru
    Petr G. Leiman
    Victor A. Kostyuchenko
    Paul R. Chipman
    Vadim V. Mesyanzhinov
    Fumio Arisaka
    Michael G. Rossmann
    Nature, 2002, 415 : 553 - 557
  • [28] GENE STRUCTURE AND FUNCTION IN HIII REGION OF BACTERIOPHAGE T4
    JINKS, JL
    HEREDITY, 1961, 16 (02) : 153 - &
  • [29] SEQUENCE OF GENE PRODUCT INTERACTION IN BACTERIOPHAGE T4 TAIL CORE ASSEMBLY
    MEEZAN, E
    WOOD, WB
    JOURNAL OF MOLECULAR BIOLOGY, 1971, 58 (03) : 685 - &
  • [30] A PROPOSED STRUCTURE OF BACTERIOPHAGE-T4 GENE PRODUCT-22 - A MAJOR PROHEAD SCAFFOLDING CORE PROTEIN
    MESYANZHINOV, VV
    SOBOLEV, BN
    MARUSICH, EI
    PRILIPOV, AG
    EFIMOV, VP
    JOURNAL OF STRUCTURAL BIOLOGY, 1990, 104 (1-3) : 24 - 31