Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-1-7
pubmed:abstractText
Lysine propionylation and butyrylation are protein modifications that were recently identified in histones. The molecular components involved in the two protein modification pathways are unknown, hindering further functional studies. Here we report identification of the first three in vivo non-histone protein substrates of lysine propionylation in eukaryotic cells: p53, p300, and CREB-binding protein. We used mass spectrometry to map lysine propionylation sites within these three proteins. We also identified the first two in vivo eukaryotic lysine propionyltransferases, p300 and CREB-binding protein, and the first eukaryotic depropionylase, Sirt1. p300 was able to perform autopropionylation on lysine residues in cells. Our results suggest that lysine propionylation, like lysine acetylation, is a dynamic and regulatory post-translational modification. Based on these observations, it appears that some enzymes are common to the lysine propionylation and lysine acetylation regulatory pathways. Our studies therefore identified first several important players in lysine propionylation pathway.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-10716917, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-11672522, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-12648672, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-14172992, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-15041175, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-15053638, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-15952748, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-16557269, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-16916647, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-17079682, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-17189186, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-17267393, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-17447894, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-17684016, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-17694074, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-17951578, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-18356920, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-18485870, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-8601308, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-8602529, http://linkedlifedata.com/resource/pubmed/commentcorrection/18753126-9194564
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1535-9484
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
45-52
pubmed:dateRevised
2010-9-21
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Molecular characterization of propionyllysines in non-histone proteins.
pubmed:affiliation
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural