Molecular and Cellular Biochemistry

, Volume 40, Issue 3, pp 173–187 | Cite as

Ubiquitin — protein conjugates

  • Harris Busch
  • Ira L. Goldknopf
Article
Received:

Summary

The data available at present indicates there are three distinct functions of ubiquitin, two of which are related to protein conjugation. The first of these has been extensively studied by our laboratory and others interested in nucleosomes and changes in chromatin states. The ubiquitin-histone (Ub-2A, Ub-2B) conjugation reaction now appears to be a very dynamic process. In the deconjugation (lyase) reaction, both the histone 2A and the ubiquitin are left intact and in a form which makes possible ready reconjugation. Accordingly, this may be a mechanism for ‘moment-to-moment’ control of the genome.

The second function in which ubiquitin is conjugated involves proteolytic activity. This activity is correlated with protein turnover. In this process, the ubiquitin-protein conjugate apparently serves as a ‘signal’ for the protease cleavage of the protein. The released ubiquitin is also intact and is probably available for reconjugation.

In the third function, ubiquitin was suggested to serve as ‘hormone’. The studies thus far have been carried out primarily on induction of T- and B-lymphocytes, reduction or delay of Coombs' positivity and reduction of spleen weight. The precise physiological role of this reported function is still unclear, particularly because the ubiquitin used was probably not the physiologically active form.

Keywords

Dynamic Process Active Form Physiological Role Proteolytic Activity Protein Turnover 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Martinus Nijhoff/Dr W. Junk Publishers 1981

Authors and Affiliations

  • Harris Busch
    • 1
  • Ira L. Goldknopf
    • 1
  1. 1.Dept. of PharmacologyBaylor College of MedicineHoustonUSA

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