Primary Structure of Mouse Liver Metallothionein -I and -II

Iy, Huang; Tsunoo, Hajime; Kimura, Masami; Nakashima, Hideki; Yoshida, Akira

doi:10.1007/978-3-0348-6493-0_8

Cited by 10 publications

(8 citation statements)

References 4 publications

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“…The positions of the introns were assigned by comparison with the mouse MT-I and human MT-II genes (15,24) and the protein sequence of mouse MT-II (21). The position of the second intron was confirmed by comparison with the sequences of the genomic and cDNA clones.…”

Section: Resultsmentioning

confidence: 99%

Regulation, linkage, and sequence of mouse metallothionein I and II genes.

Searle¹,

Davison²,

Stuart³

et al. 1984

Mol. Cell. Biol.

336

168

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The mouse metallothionein II (MT-H) gene is located -6 kilobases upstream of the MT-I gene. A comparison of the sequences of mouse MT-I and MT-II genes (as well as those of other mammals) reveals that the coding regions are highly conserved even at "silent" positions but that the noncoding regions and introns are extremely divergent between primates and rodents. There are four blocks of conserved sequences in the promoters of mouse MT-I, mouse MT-II, and human MT-IIA genes; one includes the TATAAA sequence, and another has been implicated in regulation by heavy metals. Mouse MT-I and MT-II mRNAs are induced to approximately the same extent in vivo in response to cadmium, dexamethasone, or lipopolysaccharide. Mouse MT-I and MT-II genes are regulated by metals but not by glucocorticoids after transfection into HeLa cells.

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Section: Resultsmentioning

confidence: 99%

Regulation, linkage, and sequence of mouse metallothionein I and II genes.

Searle¹,

Davison²,

Stuart³

et al. 1984

Mol. Cell. Biol.

336

168

View full text Add to dashboard Cite

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“…However, sequences involved in the copper-dependent control of gene expression are either not present in the 3.5-kb stretch upstream of the PaMt1 start codon, or the sequences associated with copper inducibility have been altered in the P. anserina transformants analyzed (see Discussion). In the heterologous yeast system, the 559-bp fragment Huang et al 1979;Durnam et al 1980), and human MT-II (Nterminal segment; Kissling and KaÈ gi 1979;Karin and Richards 1982). The boxes indicate identical amino acids and asterisks methionine residues that are removed during protein processing.…”

Section: Isolation and Sequence Analysis Of Pamt1mentioning

confidence: 99%

Molecular control of copper homeostasis in filamentous fungi: increased expression of a metallothionein gene during aging of Podospora anserina

et al. 2001

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The lifespan of the ascomycete Podospora anserina was previously demonstrated to be significantly increased in a copper-uptake mutant, suggesting that copper is a potential stressor involved in degenerative processes. In order to determine whether changes in copper stress occur in the cells during normal aging of cultures, we cloned and characterized a gene coding for a component of the molecular machinery involved in the control of copper homeostasis. This gene, PaMt1, is a single-copy gene that encodes a metallothionein of 26 amino acids. The coding sequence of PaMt1 is interrupted by a single intron. The deduced amino acid sequence shows a high degree of sequence identity to metallothioneins of the filamentous ascomycete Neurospora crassa and the basidiomycete Agaricus bisporus, and to the N-terminal portion of mammalian metallothioneins. Levels of PaMt1 transcript increase in response to elevated amounts of copper in the growth medium and during aging of wild-type cultures. In contrast, in the long-lived mutant grisea, transcript levels first increase but then decrease again. The ability of wild-type cultures to respond to exogenous copper stress via the induction of PaMt1 transcription is not affected as they grow older.

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“…Kagi et al (1974) reported extensive microheterogeneity attributable to the presence of at least two different species of MT. It is verified by the study on the amino acid sequence of MT-1 and MT-2 (Huang et al , 1977). The difference in microheterogeneity between hedgehog and rabbit MTs might depend upon the species difference.…”

Section: Discussionmentioning

confidence: 66%

Purification and characterization of hedgehog liver metallothioneins

Pan

Feng

Duan

et al. 1993

Biomedical Chromatography

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Two forms of liver metallothioneins (MTs) were purified from hedgehog exposed to zinc, using gel filtration on Sephacryl S-100 and DEAE Sepharose Fast Flow chromatography. The peptide chain weight of both MT-1 and MT-2 was found to be about 10,000, as determined by high performance liquid chromatography. This value was higher than that calculated from amino acid analysis. The amino acid composition of hedgehog liver MT-1 and MT-2 resembles that of liver to MTs from rabbit and other species. Their distinctive features include an extremely high cysteine content, about 33% of all the amino acid residues, and an absence of aromatic amino acids and histidine. In addition, a rapid method for the determination of MTs during animal tissue purification has been established. The samples were directly added in an ammoniacal solution of a Co(II) salt for recording linear sweep polarograms. By comparison with the commonly used metal determination method, our method is direct, rapid, credible and suitable for all the MTs or MT-like samples.

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Primary Structure of Mouse Liver Metallothionein -I and -II

Cited by 10 publications

References 4 publications

Regulation, linkage, and sequence of mouse metallothionein I and II genes.

Regulation, linkage, and sequence of mouse metallothionein I and II genes.

Molecular control of copper homeostasis in filamentous fungi: increased expression of a metallothionein gene during aging of Podospora anserina

Purification and characterization of hedgehog liver metallothioneins

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