Home LiteratureArticle Details
PMID: 592421 Published · ppublish English Journal Article

On the cysteine and cystine content of proteins. Differences between intracellular and extracellular proteins.

Journal of molecular evolution ·Vol. 10 ·No. 2 ·1977-11-25 ·Pages 155-60

Fahey RC, Hunt JS, Windham GC

Abstract

Analysis of published data on the cysteine and half-cystine content of proteins indicates that most intracellular proteins may be classified as sulfhydryl proteins (those containing cysteine but little or no half-cystine) and that such sulfhydryl proteins have a low cysteine content. The mean systeine content found for 32 intracellular mammalian proteins was 1.6% and intracellular proteins of many bacteria have similar or lower values. Extracellular mammalian proteins are primarily disulfide proteins (those containing half-cystine but little or no cysteine) have a high half-cystine content, the mean value found for some 34 extracellular mammalian proteins being 4.1%. This is contrasted with many of the extracellular proteins from facultative bacteria which are cyst(e)ine-free proteins, being lacking in both cysteine and half-cystine. These and related observations are interpreted in terms of the evolution of life in a reducing atmosphere and the subsequent transition to an oxidizing environment. It is suggested that disulfide proteins evolved primarily after the accumulation of oxygen in the atmosphere.

MeSH Terms
Bacterial Proteins/analysis Biological Evolution Cysteine/analysis Cystine/analysis Environment Extracellular Space/analysis Proteins/analysis
Chemicals
Bacterial Proteins Proteins Cystine Cysteine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fahey R C
Hunt J S
Windham G C
References (20)
20 references, click to expand
  1. Amino acid composition of proteins as a product of molecular evolution.
    Science. 1971 Oct 8;174(4005):150-3 PMID: 5119625
  2. Low cyst(e)ine content of bacterial extracellular proteins: its possible physiological significance.
    Nature. 1962 May 5;194:446-9 PMID: 14487664
  3. Conservation of Shannon's redundancy for proteins.
    J Mol Evol. 1974;3(3):189-208 PMID: 4851162
  4. Primary structural analysis of sulfhydryl protease inhibitors from pineapple stem.
    J Biol Chem. 1975 Mar 10;250(5):1741-50 PMID: 1112827
  5. Genetic variability maintained in a finite population due to mutational production of neutral and nearly neutral isoalleles.
    Genet Res. 1968 Jun;11(3):247-69 PMID: 5713805
  6. [Purification and characterization of an extracellular protease from Staphylococcus aureus inhibited by EDTA].
    Biochimie. 1976;58(7):793-804 PMID: 823980
  7. Purification and properties of clostridiopeptidase B (Clostripain).
    J Biol Chem. 1968 Sep 25;243(18):4683-92 PMID: 4971659
  8. Amino acid sequence of Streptomyces griseus trypsin. Cyanogen bromide fragments and complete sequence.
    Biochemistry. 1975 Mar 25;14(6):1168-77 PMID: 804314
  9. Primary structure of alpha-lytic protease: a bacterial homologue of the pancreatic serine proteases.
    Nature. 1970 Oct 31;228(5270):438-42 PMID: 5482494
  10. The elastase-like enzymes from Streptomyces griseus (pronase). Isolation and partial characterization.
    Eur J Biochem. 1971 Mar 1;19(1):90-6 PMID: 4994590
  11. The protein of human erythrocyte membranes. I. Preparation, solubilization, and partial characterization.
    J Biol Chem. 1968 Apr 25;243(8):1985-92 PMID: 5646489
  12. Malate dehydrogenases. II. Purification and properties of Bacillus subtilis, Bacillus stearothermophilus, and Escherichia coli malate dehydrogenases.
    J Biol Chem. 1967 Apr 10;242(7):1548-59 PMID: 4960671
  13. Cellular mechanisms of oxygen toxicity.
    Physiol Rev. 1968 Apr;48(2):311-73 PMID: 4870377
  14. Amino acid composition of proteins: Selection against the genetic code.
    Science. 1975 Jul 4;189(4196):50-1 PMID: 237322
  15. [The amino-acid composition of some aerobic and anaerobic bacteria].
    Zentralbl Bakteriol Orig A. 1971 May;217(1):47-62 PMID: 5091514
  16. ENZYME SYSTEMS CONTAINING ACTIVE SULFHYDRYL GROUPS. THE ROLE OF GLUTATHIONE.
    Science. 1943 Apr 16;97(2520):356-8 PMID: 17843092
  17. Non-Darwinian evolution.
    Science. 1969 May 16;164(3881):788-98 PMID: 5767777
  18. Counter-examples to a neutralist hypothesis.
    J Mol Evol. 1976 Apr 9;7(3):185-95 PMID: 933175
  19. A statistical analysis of the amino acid compositions of proteins.
    Int J Pept Protein Res. 1973;5(2):109-17 PMID: 4763356
  20. Deviations from compositional randomness in eukaryotic and prokaryotic proteins: the hypothesis of selective-stochastic stability and a principle of charge conservation.
    J Mol Evol. 1975 Mar 24;4(4):277-306 PMID: 173858
Article Info
Journal
Journal of molecular evolution
Abbr.
J Mol Evol
ISSN
0022-2844
Published
1977-11-25
Pages
155-60
Language
English
Region
Germany
NLM ID
0360051
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com