Cloning and identification of a novel cDNA which encodes a putative protein with a DnaJ domain and a thioredoxin active motif, human macrothioredoxin

Shao Hua Gu, Jin Zhong Chen, Kang Ying, Shu Wang, Wei Jin, Ji Qian, En Peng Zhao, Yi Xie, Yu Min Mao

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

A 3345 bp cDNA was isolated from the fetal brain cDNA library by high throughput cDNA sequencing. The cDNA with an open reading fragment (ORF) of 2241 bp encodes a 747 amino acids putative protein with a DnaJ N-terminus domain and four thioredoxin active sets. So it is named human macrothioredoxin (hMTHr).4 We used Northern blot to detect a band with a length of about 5 kb, which was ubiquitously expressed in human adult tissues with different intensities. The expression pattern was verified by RT-PCR, revealing that the transcripts were ubiquitously expressed in fetal tissues and human tumor tissues also. The transcripts in fetal tissues were more numerous than in adult tissues. The transcripts were high in adult testis, adult pancreas, fetal thymus, and fetal kidney. We have found three splice isoforms with lengths of 3483, 3345, and 2982 bp in the sequencing analysis of the RT-PCR products. They encode three putative proteins with 793, 747, and 275 amino acids, respectively. The first two putative proteins contain a DnaJ domain and four thioredoxin domains. The third putative protein only contains an N-terminus DnaJ domain and one thioredoxin active set. Blast analysis against the NCBI database revealed that the gene spans a genome sequence of about 75 kb that contains at least 25 exons and is located in human chromosome 2q32.1. The organization of the functional motifs of hMTHr suggests that the protein might be a member of a molecular chaperone family.

Original languageEnglish (US)
Pages (from-to)245-253
Number of pages9
JournalBiochemical Genetics
Volume41
Issue number7-8
DOIs
StatePublished - Aug 2003
Externally publishedYes

Fingerprint

Thioredoxins
Cloning
Organism Cloning
molecular cloning
Complementary DNA
Tissue
protein
Proteins
proteins
Fetus
amino acid
Genes
reverse transcriptase polymerase chain reaction
Amino Acids
Thymus
Polymerase Chain Reaction
molecular chaperones
amino acids
Molecular Chaperones
Human Chromosomes

Keywords

  • Chaperone
  • DnaJ
  • Human macrothioredoxin (hMTHr)
  • Splice isoform
  • Thioredoxin

ASJC Scopus subject areas

  • Biochemistry
  • Genetics

Cite this

Cloning and identification of a novel cDNA which encodes a putative protein with a DnaJ domain and a thioredoxin active motif, human macrothioredoxin. / Gu, Shao Hua; Chen, Jin Zhong; Ying, Kang; Wang, Shu; Jin, Wei; Qian, Ji; Zhao, En Peng; Xie, Yi; Mao, Yu Min.

In: Biochemical Genetics, Vol. 41, No. 7-8, 08.2003, p. 245-253.

Research output: Contribution to journalArticle

Gu, Shao Hua ; Chen, Jin Zhong ; Ying, Kang ; Wang, Shu ; Jin, Wei ; Qian, Ji ; Zhao, En Peng ; Xie, Yi ; Mao, Yu Min. / Cloning and identification of a novel cDNA which encodes a putative protein with a DnaJ domain and a thioredoxin active motif, human macrothioredoxin. In: Biochemical Genetics. 2003 ; Vol. 41, No. 7-8. pp. 245-253.
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AU - Qian, Ji

AU - Zhao, En Peng

AU - Xie, Yi

AU - Mao, Yu Min

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