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EMI, a novel cysteine‐rich domain of EMILINs and other extracellular proteins, interacts with the gC1q domains and participates in multimerization
Author(s) -
Doliana Roberto,
Bot Simonetta,
Bonaldo Paolo,
Colombatti Alfonso
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02140-2
Subject(s) - chemistry , emi , microbiology and biotechnology , cysteine , domain (mathematical analysis) , extracellular , biophysics , biology , biochemistry , computer science , electromagnetic interference , telecommunications , mathematical analysis , mathematics , enzyme
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 EMI 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.