MAPPING OF THE ACTOMYOSIN INTERFACES

被引：4

作者：

ELDIN, P ^{[1
]}

LECUNFF, M ^{[1
]}

VOSBERG, HP ^{[1
]}

MORNET, D ^{[1
]}

LEGER, JJ ^{[1
]}

机构：

[1] MAX PLANCK INST,W-6350 BAD NAUHEIM,GERMANY

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1994年 / 91卷 / 07期

关键词：

D O I：

10.1073/pnas.91.7.2772

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Recombinant DNA methods were used to obtain soluble, undenatured fragments of the heavy chain of myosin subfragment 1 (S-1). These fragments were of preselected lengths and could include protease-sensitive segments that are destroyed when other preparation methods are used. Actin binding by each of the three contiguous segments (residues 1-248, 249-524, and 518-722, essentially spanning the entire S-1 heavy chain) was demonstrated. ATP binding, comparable to that of native S-1, was obtained only with a segment consisting of residues 1-524. Competition among the various fragments for actin was also studied. The data are discussed in relation to the recently reported resolved structure of S-1 [Rayment, I., Rypnieski, R. W., Schmidt-Base, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G. & Holden, H. M. (1993) Science 261, 50-58].

引用

页码：2772 / 2776

页数：5

共 42 条

[1] SPECTROSCOPIC ISOLATION OF ES COMPLEXES OF MYOSIN SUBFRAGMENT-1 ATPASE BY FLUORESCENCE QUENCHING [J].