Identification of protein substrates for transglutaminase in Caenorhabditis elegans

A. Mádi, Z. Kele, T. Janáky, Mária Punyiczki, L. Fésüs

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Transglutaminase-dependent cross-linking of proteins leads to protein polymerisation that confers stability as well as resistance to mechanical disruption and chemical attack. Various transglutaminases have been implicated in a wide range of biological phenomena occurring in both extracellular and intracellular compartments, but further clarification of the physiological role of these enzymes requires identification of possible substrate molecules. Here we report the detection, purification, and identification of two proteins, enolase and ATP synthase α subunit as glutamine donor protein substrates for the transglutaminase of the nematode Caenorhabditis elegans.

Original languageEnglish
Pages (from-to)964-968
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume283
Issue number4
DOIs
Publication statusPublished - 2001

Fingerprint

Transglutaminases
Caenorhabditis elegans
Substrates
Proteins
Chemical attack
Biological Phenomena
Phosphopyruvate Hydratase
Glutamine
Polymerization
Purification
Adenosine Triphosphate
Molecules
Enzymes

Keywords

  • Caenorhabditis elegans
  • Enolase
  • Mitochondrial ATP synthase
  • Substrate
  • Transglutaminase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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T1 - Identification of protein substrates for transglutaminase in Caenorhabditis elegans

AU - Mádi, A.

AU - Kele, Z.

AU - Janáky, T.

AU - Punyiczki, Mária

AU - Fésüs, L.

PY - 2001

Y1 - 2001

N2 - Transglutaminase-dependent cross-linking of proteins leads to protein polymerisation that confers stability as well as resistance to mechanical disruption and chemical attack. Various transglutaminases have been implicated in a wide range of biological phenomena occurring in both extracellular and intracellular compartments, but further clarification of the physiological role of these enzymes requires identification of possible substrate molecules. Here we report the detection, purification, and identification of two proteins, enolase and ATP synthase α subunit as glutamine donor protein substrates for the transglutaminase of the nematode Caenorhabditis elegans.

AB - Transglutaminase-dependent cross-linking of proteins leads to protein polymerisation that confers stability as well as resistance to mechanical disruption and chemical attack. Various transglutaminases have been implicated in a wide range of biological phenomena occurring in both extracellular and intracellular compartments, but further clarification of the physiological role of these enzymes requires identification of possible substrate molecules. Here we report the detection, purification, and identification of two proteins, enolase and ATP synthase α subunit as glutamine donor protein substrates for the transglutaminase of the nematode Caenorhabditis elegans.

KW - Caenorhabditis elegans

KW - Enolase

KW - Mitochondrial ATP synthase

KW - Substrate

KW - Transglutaminase

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