Molecular characterization and expression of a putative ATPase domain from Eimeria tenella

Saw Peng Chong, Mohd Sanusi Jangi, Kiew Lian Wan

Research output: Contribution to journalArticle

Abstract

VCP (Valosin-Containing Protein), a member of the AAA (ATPases Associated to a variety of cellular Activities) family of proteins, possesses a duplicated highly conserved ATPase domain. An expressed sequence tag (EST), representing a clone from the Eimeria tenella merozoite cDNA library, was found to have high similarity to VCP genes from other organisms. A complete sequence derived from the corresponding clone (designated eth060) shows amino acid identity of 42-62% with other members of the VCP subfamily. Sequence analysis identified a putative ATPase domain in the eth060 sequence. This domain was PCR-amplified using gene-specific primers and cloned into a pBAD/Thio-TOPO expression vector. Expression in Escherichia coli demonstrated that the putative ATPase domain, which consists of 414 amino acid residues, produced a fusion protein of approximately 60 kDa in size.

Original languageEnglish
Pages (from-to)123-128
Number of pages6
JournalJournal of Biochemistry, Molecular Biology and Biophysics
Volume6
Issue number2
DOIs
Publication statusPublished - Apr 2002

Fingerprint

Eimeria tenella
Adenosine Triphosphatases
Clone Cells
Genes
Merozoites
Amino Acids
Expressed Sequence Tags
Gene Library
Escherichia coli
Sequence Analysis
Proteins
Fusion reactions
Polymerase Chain Reaction
CDC48 protein

Keywords

  • AAA family
  • EST
  • Merozoite
  • VCP

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Biophysics

Cite this

Molecular characterization and expression of a putative ATPase domain from Eimeria tenella. / Chong, Saw Peng; Jangi, Mohd Sanusi; Wan, Kiew Lian.

In: Journal of Biochemistry, Molecular Biology and Biophysics, Vol. 6, No. 2, 04.2002, p. 123-128.

Research output: Contribution to journalArticle

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