Caveolin-1 binding motif of α-hemolysin:: its role in stability and pore formation

被引：45

作者：

Pany, S ^{[1
]}

Vijayvargia, R ^{[1
]}

Krishnasastry, MV ^{[1
]}

机构：

[1] Natl Ctr Cell Sci, Pune 411007, Maharashtra, India

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 322卷 / 01期

关键词：

alpha-hemolysin; caveolin-1 binding motif; scaffolding domain; hetero-oligomerization; fluorescence studies; ANS binding;

D O I：

10.1016/j.bbrc.2004.07.073

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

We have identified a nine amino sequence in alpha-hemolysin (alpha-HL) of Staphylococcus aureus, which binds Caveolin-1. Surface plasmon resonance studies clearly show a concentration dependent interaction of alpha-HL with the scaffolding domain of Caveolin-1. Mutants of alpha-HL, devoid of Caveolin-1 recognition motif, exhibit an a-HL like proteinase K digestion profile but the resultant 'half-like' domains are highly susceptible to further proteolysis. They also had the same intrinsic fluorescence emission maxima as the native alpha-HL indicating normal folding. However, these mutants bind 1-anilino-8-naphthalene sulfonic acid probably due to exposure of their hydrophobic core. Moreover, these mutants are non-lytic and do not undergo conformational changes on rabbit RBC membrane surface. Purified Caveolin-1 blocks the hemolysis of RBCs by alpha-HL. Our studies indicate that the Caveolin-1 binding motif of alpha-HL provides stability and shields the hydrophobic core of alpha-HL. The motif also acts as trigger point for initiation of conformational changes. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：29 / 36

页数：8

共 27 条

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