Structure and ligand of a histone acetyltransferase bromodomain
Article Abstract:
The bromodomains contained in almost all known histone-acetyltransferase-associated transcriptional co-activators seem to be acetyl-lysine-binding domains. They are therefore the first protein modules to show such interactions. The bromodomain/acetyl-lysine recognition could control protein-protein interactions by lysine acetylation. Bromodomain-acetyl-lysine binding could also play a significant role in the assembly and activity of multi-protein complexes in transcriptional activation.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Helices sculpt membrane
Article Abstract:
Specialized 'coat' proteins wrap up a small area of the lipid membrane, shaping it into a bulging 'bud' and gathers the proteins due to be transported inside and the bud detaches from the membrane a stage called fission to form a bubble-like 'vesicle' loaded with cargo. This structure initiates buds of one type vesicle by thrusting one of its helices into the membrane, causing it to look like balloon.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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