EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gC1q domains and participates in multimerization

Roberto Doliana, Simonetta Bot, Paolo Bonaldo, Alfonso Colombatti

Research output: Contribution to journalArticlepeer-review

Abstract

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. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)164-168
Number of pages5
JournalFEBS Letters
Volume484
Issue number2
DOIs
Publication statusPublished - Nov 3 2000

Keywords

  • Elastic fiber
  • Extracellular matrix
  • Protein domain
  • Protein interaction
  • Two-hybrid system

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint Dive into the research topics of 'EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gC1q domains and participates in multimerization'. Together they form a unique fingerprint.

Cite this