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Home/Equine Research Bank/Proc Natl Acad Sci U S A/Amino-acid sequence of equine renal metallothionein-1B.
Proceedings of the National Academy of Sciences of the United States of America1976; 73(10); 3413-3417; doi: 10.1073/pnas.73.10.3413

Amino-acid sequence of equine renal metallothionein-1B.

Abstract: The amino-acid sequence of a metallothionein is reported. Metallothionein is a widely distributed, extremely cysteine-rich, low-molecular-weight protein containing large amounts of cadmium and/or zinc. Metallothionein-1B is one of the two prinicipal variants occurring in equine kidney cortex. The single-chain protein contains 61 amino acids and has the composition Cys20 Ser8Lys7Arg1Ala7Gly5Val3Asp2Asn1-Glu1Gln2Pro2Thr1Met1(Cd + Zn)7. Its amino-terminal residue is N-acetylmethionine. The sequence shows distinct clustering of the twenty cysteinyl residues into seven groups separated by stretches of at least three other residues. Within these groups the cysteines occur seven times in alternating Cys-X-Cys sequences and three times each in Cys-Cys and Cys-X-X-Cys sequences, where X is an amino acid other than cysteine. Another unique feature is the close association of serine and the basic amino acids with cysteine, as manifested by the occurrence of seven Ser-Cys, four Cys-Lys, one Cys-Arg, and three Lys-Cys sequences. These findings are in agreement with the previous suggestion that metallothionein has structurally defined metal-binding sites, most of which contain three cysteinyl residues as the principal metal-binding ligands. The charge difference between the metal-free and the metal-containing protein is consistent with the formation of negatively charged trimercaptide complexes with cadmium and/or zinc ions. The possible additional involvement of serine and the basic amino acids in metal binding is discussed.
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Publication Date: 1976-10-01 PubMed ID: 1068454PubMed Central: PMC431125DOI: 10.1073/pnas.73.10.3413Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research is about the amino-acid sequence of a protein called metallothionein-1B that occurs in the kidney cortex of horses. The protein is rich in cysteine and often carries large amounts of zinc and/or cadmium.

Protein Description

  • The study reports the sequence for a type of protein known as metallothionein, specifically metallothionein-1B. This protein is prominent in the kidney cortex of horses.
  • Metallothionein is a low-molecular-weight protein characterized by high cysteine content. It also carries significant volumes of cadmium and/or zinc.
  • The single-chain protein metallothionein-1B contains 61 amino acids; 20 of them are cysteines (Cys). CySteine is especially significant since it is usually involved in binding to metal ions.
  • The rest of the sequence consists of other amino acids: Ser 8, Lys 7, Arg 1, Ala 7, Gly 5, Val 3, Asp 2, Asn 1, Glu 1, Gln 2, Pro 2, Thr 1, and Met 1. It also has seven metal ions (either cadmium or zinc).

Protein Sequence Analysis

  • The study reveals a distinct pattern where the cysteine sources are separated into seven clusters with gaps of at least three other residues.
  • Within these cysteine groups, the Cys-X-Cys sequence structure appears seven times where X is an amino acid different from Cys. This structure is crucial for understanding the protein’s interaction with metal ions.
  • The sequence analysis also reveals a close association between serine and the basic amino acids with cysteine, as indicated by occurrences of Ser-Cys, Cys-Lys, Cys-Arg, and Lys-Cys sequences. This suggests a potential role of these amino acids in metal binding.

Implications

  • This study’s significance lies in the proposed structure of metallothionein, indicating that these proteins have defined metal-binding sites, most containing three key Cys residues.
  • The researchers also discuss the possibility of serine and the basic amino acids playing a role in metal binding, based on the observed sequence relationships. This implies that other amino acids might be relevant in the formation of metal protein complexes besides cysteine.
  • Understanding metallothionein structure is key to deciphering its function and role in important biological processes including detoxification of heavy metals, regulation of zinc and copper levels, and protection against oxidative damage.

Cite This Article

APA
Kojima Y, Berger C, Vallee BL, Ku00e4gi JH. (1976). Amino-acid sequence of equine renal metallothionein-1B. Proc Natl Acad Sci U S A, 73(10), 3413-3417. https://doi.org/10.1073/pnas.73.10.3413

Publication

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
NlmUniqueID: 7505876
Country: United States
Language: English
Volume: 73
Issue: 10
Pages: 3413-3417

Researcher Affiliations

Kojima, Y
    Berger, C
      Vallee, B L
        Ku00e4gi, J H

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • Binding Sites
          • Cysteine
          • Horses
          • Kidney / analysis
          • Metalloproteins
          • Metallothionein

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          Citations

          This article has been cited 46 times.
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