Chemical and genetic strategies for manipulating polyubiquitin chain structure.
Ubiquitin can be conjugated to lysine residues of other ubiquitin molecules to form polymers called polyubiquitin chains. Ubiquitin has seven lysine residues, creating the potential for seven distinct types of chains, at least five of which have been observed in vitro or in vivo. A subset of these chains mediates substrate targeting to proteasomes, whereas other types of chains have been implicated in nonproteolytic signaling pathways. In this chapter, we outline chemical and genetic strategies that can be used to deduce (or control) the structures of polyubiquitin chains in vitro and in living cells.
Volk
Sara
S
Department of Biochemistry and Molecular Biology, Johns Hopkins University, Baltimore, Maryland, USA.
Wang
Min
M
Pickart
Cecile M
CM
D000595:Amino Acid Sequence; D001120:Arginine / Q000235:genetics; D008239:Lysine / Q000235:genetics; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D017354:Point Mutation; D025821:Polyubiquitin / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D025821:Polyubiquitin; D001120:Arginine; D008239:Lysine