REASSEMBLY OF THE BACTERIOPHAGE-T4 TAIL FROM THE COREBASEPLATE AND THE MONOMERIC SHEATH PROTEIN P18 - COOPERATIVE ASSOCIATION PROCESS

被引:26
作者
ARISAKA, F
TSCHOPP, J
VANDRIEL, R
ENGEL, J
机构
[1] CH-4056 Basel
[2] CH-4056 Basel
基金
俄罗斯科学基金会;
关键词
D O I
10.1016/0022-2836(79)90266-3
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 reassociation of the monomeric sheath protein, the product of gene 18, with the core-baseplate was investigated by analytical ultracentrifugation, light-scattering and electron microscopy. The following conclusions are reached: (1) monomeric P18 molecules are in equilibrium with the extended tail sheath; (2) the association process is co-operative and the critical concentration of P18 is about 0.4 μm in the presence of 0.1 m-KCl in 1 mm-potassium phosphate buffer (pH 7.0 at 20 °C); (3) binding of P18 to the baseplate-core junction is the initial stop in extended sheath formation; (4) slow, irreversible polysheath formation competes with the assembly of extended sheath, but the latter is kinetically much more favored. Model calculations on the isotherm of the sheath formation and on the length distribution strongly suggest a rate-limiting nucleation step, and a distinctly strong binding of the last annulus of the sheath to the core-baseplate. © 1979.
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页码:369 / 386
页数:18
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