Tilapia and human CLIC2 structures are highly conserved

Biochem Biophys Res Commun. 2018 Jan 8;495(2):1752-1757. doi: 10.1016/j.bbrc.2017.11.189. Epub 2017 Dec 2.

Abstract

Chloride intracellular channels (CLICs) exist in soluble and membrane bound forms. We have determined the crystal structure of soluble Clic2 from the euryhaline teleost fish Oreochromis mossambicus. Structural comparison of tilapia and human CLIC2 with other CLICs shows that these proteins are highly conserved. We have also compared the expression levels of clic2 in selected osmoregulatory organs of tilapia, acclimated to freshwater, seawater and hypersaline water. Structural conservation of vertebrate CLICs implies that they might play conserved roles. Also, tissue-specific responsiveness of clic2 suggests that it might be involved in iono-osmoregulation under extreme conditions in tilapia.

Keywords: CLIC2; CXXC motif; Crystal structure; Glutaredoxin fold; Glutathione S-Transferase (GST) fold.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chloride Channels / chemistry*
  • Chloride Channels / genetics*
  • Chloride Channels / metabolism
  • Conserved Sequence
  • Fish Proteins / chemistry*
  • Fish Proteins / genetics*
  • Fish Proteins / metabolism
  • Humans
  • Models, Molecular
  • Osmoregulation / genetics
  • Osmoregulation / physiology
  • Phylogeny
  • Protein Conformation
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Salinity
  • Sequence Homology, Amino Acid
  • Tilapia / genetics*
  • Tilapia / physiology

Substances

  • CLIC2 protein, human
  • Chloride Channels
  • Fish Proteins
  • RNA, Messenger