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Acetylation of Histone Lysine Residues
Lysine rich tail binds tightly to DNA, blocks DNA access for transcription. Acetylation of these lysines unblocks the DNA.
Acetylation as a Transducing Signal
Acetylation of a histone at a location on a protein or other molecule may eliminate/create recognition sites
Acetylation effects on a Nonhistone protein
Affects overall activity of protein broadly
Writers
Enzymes that add modifications to proteins
Erasers
enzymes which remove the modification
Readers
proteins that recognize and bind to the modification
Histone acetylation correlates to..
gene activation
Trimethylation of H3K4 (H3K4me3 in promoter regions) and H3K36 (H3K36me3 in transcribed regions/gene bodies) correlates to…
gene activation
Trimethylation of H3K9(me3) correlates to…
heterochromatin (transcriptional) gene repression
Trimethylation of H3K27(me3) correlates to…
polycomb-mediated gene repression (Polycomb Repressive Complexes 1 (reader), 2(reader and writer of me3) [PRC 1,2])
H3K4me1 and H3K27ac are seen at..
active transcriptional enhancers
ChIP-seq
Chromatin-immunoprecipitation sequencing. Identifies protein binding sites and enable analysis of transcription factors, histone modifications, and chromatin states
SAM
S-Adenosyl Methionine, Histone methylase cofactor
Acetyl-CoA
Acetyl Coenzyme A. Histone acetylase cofactor
Rpd3
Histone-deacetylase. No cofactor needed
LSD-1
Demethylase that uses FAD as a cofactor
JHDM
Demethylase that uses Fe(II) as a cofactor