Evolutionary mode of metallothioneins inferred from Cd-MT genes of tetrahymena

Ming Liang Wan; Wei Song Feng; Wei Miao; Ming Hong Wong

doi:10.1007/bf02832440

Evolutionary mode of metallothioneins inferred from Cd-MT genes of tetrahymena

Ming Liang Wan^*, Wei Song Feng, Wei Miao, Ming Hong Wong

^*Corresponding author for this work

Department of Biology

Research output: Contribution to journal › Journal article › peer-review

2 Citations (Scopus)

Abstract

From Tetrahymena thermophila (strain BF5), the coding region of Cd-MT gene was cloned and sequenced, and identified as MTT1 isoform. A serial duplicate structure is discovered in its amino acid sequence, which separates the coding region into three parts (Part 1: 7-61; Part 2: 64-118; Part 3: 122-162). The alignments among them and comparison with the corresponding parts of MT1 isoform suggest that MT1 and MTT1 isoforms both come from the same ancient gene that is homologous to Part 1, and Cd-MTs of Tetrahymena are aroused by such ancient gene duplication. The prediction of secondary structures and the analysis of the disulfide-bonding state of cysteine show that there are a lot of differences between MT1 and MTT1 isoforms, which maybe relate to their function mechanism.

Original language	English
Pages (from-to)	925-930
Number of pages	6
Journal	Wuhan University Journal of Natural Sciences
Volume	10
Issue number	5
DOIs	https://doi.org/10.1007/bf02832440
Publication status	Published - Sept 2005

Scopus Subject Areas

General

User-Defined Keywords

Evolutionary mode
Gene duplication
Metal-binding sites
Metallothioneins
Protein spatial structure
Tetrahymena thermophila

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10.1007/bf02832440

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title = "Evolutionary mode of metallothioneins inferred from Cd-MT genes of tetrahymena",

abstract = "From Tetrahymena thermophila (strain BF5), the coding region of Cd-MT gene was cloned and sequenced, and identified as MTT1 isoform. A serial duplicate structure is discovered in its amino acid sequence, which separates the coding region into three parts (Part 1: 7-61; Part 2: 64-118; Part 3: 122-162). The alignments among them and comparison with the corresponding parts of MT1 isoform suggest that MT1 and MTT1 isoforms both come from the same ancient gene that is homologous to Part 1, and Cd-MTs of Tetrahymena are aroused by such ancient gene duplication. The prediction of secondary structures and the analysis of the disulfide-bonding state of cysteine show that there are a lot of differences between MT1 and MTT1 isoforms, which maybe relate to their function mechanism.",

keywords = "Evolutionary mode, Gene duplication, Metal-binding sites, Metallothioneins, Protein spatial structure, Tetrahymena thermophila",

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T1 - Evolutionary mode of metallothioneins inferred from Cd-MT genes of tetrahymena

AU - Wan, Ming Liang

AU - Feng, Wei Song

AU - Miao, Wei

AU - Wong, Ming Hong

PY - 2005/9

Y1 - 2005/9

N2 - From Tetrahymena thermophila (strain BF5), the coding region of Cd-MT gene was cloned and sequenced, and identified as MTT1 isoform. A serial duplicate structure is discovered in its amino acid sequence, which separates the coding region into three parts (Part 1: 7-61; Part 2: 64-118; Part 3: 122-162). The alignments among them and comparison with the corresponding parts of MT1 isoform suggest that MT1 and MTT1 isoforms both come from the same ancient gene that is homologous to Part 1, and Cd-MTs of Tetrahymena are aroused by such ancient gene duplication. The prediction of secondary structures and the analysis of the disulfide-bonding state of cysteine show that there are a lot of differences between MT1 and MTT1 isoforms, which maybe relate to their function mechanism.

AB - From Tetrahymena thermophila (strain BF5), the coding region of Cd-MT gene was cloned and sequenced, and identified as MTT1 isoform. A serial duplicate structure is discovered in its amino acid sequence, which separates the coding region into three parts (Part 1: 7-61; Part 2: 64-118; Part 3: 122-162). The alignments among them and comparison with the corresponding parts of MT1 isoform suggest that MT1 and MTT1 isoforms both come from the same ancient gene that is homologous to Part 1, and Cd-MTs of Tetrahymena are aroused by such ancient gene duplication. The prediction of secondary structures and the analysis of the disulfide-bonding state of cysteine show that there are a lot of differences between MT1 and MTT1 isoforms, which maybe relate to their function mechanism.

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KW - Metal-binding sites

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KW - Protein spatial structure

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Evolutionary mode of metallothioneins inferred from Cd-MT genes of tetrahymena

Abstract

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