Abstract
Ubiquitin is a small protein that was initially found to function as a tag that can be covalently attached to proteins to mark them for destruction by a multisubunit, adenosine 5'-triphosphate-dependent protease called the proteasome. Ubiquitin is now emerging as a key regulator of eukaryotic messenger RNA synthesis, a process that depends on the RNA synthetic enzyme RNA polymerase II and the transcription factors that control its activity. Ubiquitin controls messenger RNA synthesis not only by mechanisms involving ubiquitin-dependent destruction of transcription factors by the proteasome, but also by an intriguing collection of previously unknown and unanticipated mechanisms that appear to be independent of the proteasome.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
-
Review
MeSH terms
-
Animals
-
Cysteine Endopeptidases / metabolism
-
Gene Expression Regulation
-
Ligases / metabolism
-
Models, Genetic
-
Multienzyme Complexes / metabolism
-
Proteasome Endopeptidase Complex
-
Protein Structure, Tertiary
-
RNA Polymerase II / metabolism
-
RNA, Messenger / biosynthesis*
-
RNA, Messenger / genetics
-
Trans-Activators / chemistry
-
Trans-Activators / metabolism
-
Transcription Factors / chemistry
-
Transcription Factors / metabolism*
-
Transcription, Genetic*
-
Transcriptional Activation
-
Ubiquitin / chemistry
-
Ubiquitin / metabolism*
-
Ubiquitin-Protein Ligases
Substances
-
Multienzyme Complexes
-
RNA, Messenger
-
Trans-Activators
-
Transcription Factors
-
Ubiquitin
-
Ubiquitin-Protein Ligases
-
RNA Polymerase II
-
Cysteine Endopeptidases
-
Proteasome Endopeptidase Complex
-
Ligases