By Avram Hershko (auth.), Jan-Michael Peters, J. Robin Harris, Daniel Finley (eds.)

The final a number of years were a landmark interval within the ubiquitin box. The breadth of ubiquitin's roles in mobilephone biology was once first sketched, and the significance of ubiquitin-dependent proteolysis as a regulatory mechanism won basic popularity. the various strands of labor that ended in this new belief are re­ counted during this publication. A end result of this development is that the sector has grown dramatically because the first e-book on ubiquitin used to be released nearly a decade in the past [M. Rechsteiner (ed. ), Ubiquitin, Plenum Press, 1988]. during this span, scholars of the telephone cycle, transcription, sign transduction, protein sorting, neuropathology, melanoma, virology, and immunology have tried to chart the function of ubi hand over in of their specific experimental platforms, and this integration of the sector into cellphone biology as a complete keeps at a striking velocity. we are hoping that for lively researchers within the box in addition to for novices and people at the fence, this publication will end up invaluable for its breadth, old standpoint, and sensible advice. Structural information at the moment are to be had on a number of the parts of the ubiquitin pathway. The constructions have supplied easy insights into the bizarre biochemical mechanisms of ubiquitination and proteasome-mediated proteolysis. simply because high-speed special effects can show constructions extra successfully than print media, we now have supplemented the figures of the booklet with a global site that could show the buildings in a versatile, viewer-controlled format.

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The brief discussion below is limited to UbH proteins for which functional information is available. There are many other UbH proteins in databases; a few of these are included in Table I. 1. lb). 1a. Viral Ubiquitin. Although the baculovirus UbH protein, known as vUb, is 79% identical to ubiquitin (Guarino, 1990; Table I), the two known baculovirus ubiquitins are more similar to each other than to animal ubiquitin (see Reilly and Guarino, 1996). This suggests that vUh has evolved to perform a specific function(s), but the nature of this function is unclear.

References: (I) Butt et al. (1988); (2) Hodgins et al. (1992); (3) Ecker et al. (1987); (4) Pickart et al. (1994); (5) Wilkinson et al. (1995); (6) Amason and Ellison (1994); (7) Pickart et al. (1992); (8) Spence et al. (1995); (9) Chau et al. (1989); (10) Finley et al. (1994); (II) Johnson et al. (1992); (12) Chau et al. (1989); (13) Baboshina and Haas (1996); (14) Burch and Haas (1994); (15) Beal et al. (1996); (16) Johnson et al. (1995). 32 • Cecile M. Pickart the structure and function of polyubiquitin chains are discussed further in Sections 3 and 4.

2. , 1984). , 1987). Polyubiquitin genes are universally distributed, although the number of repeats and the identity of the extra amino acid vary widely. In general, these genes provide ubiquitin under conditions of stress. , 1987). Synthesis as a polyprotein increases the efficiency of ubiquitin production, as processing of the linear polyubiquitin protein, and removal of the extra residue from the C-terminal ubiquitin unit, are essentially cotranslational. , 1984, 1987). 2. , 1987). Other genes, known as VBIl through VBI3, supply most of the ubiquitin for vegetative growth.

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