EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gClq domains and participates in multimerization

被引:101
作者
Doliana, R
Bot, S
Bonaldo, P
Colombatti, A [1 ]
机构
[1] Natl Canc Inst, IRCCS, CRO, Div Oncol Sperimentale 2, I-33081 Aviano, Italy
[2] Univ Padua, Dipartimento Istol & Microbiol, I-35100 Padua, Italy
[3] Univ Udine, Dipartimento Sci & Tecnol Biomed, I-33100 Udine, Italy
关键词
extracellular matrix; elastic fiber; protein domain; protein interaction; two-hybrid system;
D O I
10.1016/S0014-5793(00)02140-2
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 N-terminal cysteine-rich domain (EMI domain) of EMILIN-1 is a new protein domain that is shared with two proteins (multimerin and EMILIN-2) and with four additional database entries. The ERI domains are always located at the N-terminus, have a common gene organization, and belong to proteins that are forming or are compatible with multimer formation. The potential role of the EMI domain in the assembly of EMILIN-1 was investigated by the two-hybrid system. No reporter gene activity was detected when EMI-1 was co-transformed with the C-terminal gC1q-1 domain excluding a head-to-tail multimerization: conversely, a strong interaction was detected when the EMI-1 domain was co-transformed with the gC1q-2 domain of EMILIN-2. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:164 / 168
页数:5
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