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

FEBS Lett. 2000 Nov 3;484(2):164-8. doi: 10.1016/s0014-5793(00)02140-2.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biopolymers / metabolism
  • Cell Line
  • Complement C1q / chemistry
  • Complement C1q / metabolism*
  • Extracellular Matrix / metabolism
  • Humans
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / metabolism*
  • Molecular Sequence Data
  • Protein Conformation
  • Saccharomyces cerevisiae
  • Sequence Homology, Amino Acid

Substances

  • Biopolymers
  • Membrane Glycoproteins
  • elastin microfibril interface located protein
  • Complement C1q