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- W1997029250 abstract "Despite the fact that histone H2A ubiquitination affects about 10-15% of this histone in most eukaryotic cells, histone ubiquitination is among one of the less-well-characterized post-translational histone modifications. Nevertheless, some important observations have been made in recent years. Whilst several enzymes had been known to ubiquitinate histones in vitro, recent studies in yeast have led to the unequivocal identification of the enzyme responsible for this post-translational modification in this organism. A strong functional co-relation to meiosis and spermiogenesis has also now been well documented, although its participation in other functional aspects of chromatin metabolism, such as transcription or DNA repair, still remains rather speculative and controversial. Because of its nature, histone ubiquitination represents the most bulky structural change to histones and as such it would be expected to exert an important effect on chromatin structure. Past and recent structural studies, however, indicate a surprising lack of effect of (H2A/H2B) ubiquitination on nucleosome architecture and of uH2A on chromatin folding. These results suggest that this modification may serve as a signal for recognition by functionally relevant trans-acting factors and/or operate synergistically in conjunction with other post-translational modifications such as for instance acetylation." @default.
- W1997029250 created "2016-06-24" @default.
- W1997029250 creator A5001104135 @default.
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- W1997029250 creator A5052581562 @default.
- W1997029250 creator A5089836373 @default.
- W1997029250 date "2002-01-29" @default.
- W1997029250 modified "2023-10-09" @default.
- W1997029250 title "Histone ubiquitination: a tagging tail unfolds?" @default.
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- W1997029250 doi "https://doi.org/10.1002/bies.10038" @default.
- W1997029250 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11835281" @default.
- W1997029250 hasPublicationYear "2002" @default.
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