Linked Life Data

20818827

Source:http://linkedlifedata.com/resource/pubmed/id/20818827

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2010-11-5
pubmed:abstractText
Protein hydroxylation at proline and lysine residues is known to have important effects on cellular functions, such as the response to hypoxia. However, protein hydroxylation at tyrosine residues (called protein-bound 3,4-dihydroxy-phenylalanine (PB-DOPA)) has not been carefully examined. Here we report the first proteomics screening of the PB-DOPA protein substrates and their sites in Escherichia coli and human mitochondria by nano-liquid chromatography/tandem mass spectrometry (nano-LC/MS/MS) and protein sequence alignment using the PTMap algorithm. Our study identified 67 novel PB-DOPA sites in 43 E. coli proteins and 9 novel PB-DOPA sites in 7 proteins from HeLa mitochondria. Bioinformatics analysis indicates that the structured region is more favored than the unstructured regions of proteins for the PB-DOPA modification. The PB-DOPA substrates in E. coli were dominantly enriched in proteins associated with carbohydrate metabolism. Our study showed that PB-DOPA may be involved in regulation of the specific activity of certain evolutionarily conserved proteins such as superoxide dismutase and glyceraldehyde 3-phosphate dehydrogenase, suggesting the conserved nature of the modification among distant biological species. The substrate proteins identified in this study offer a rich source for determining their regulatory enzymes and for further characterization of the possible contributions of this modification to cellular physiology and human diseases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1535-3907
pubmed:author
pubmed:issnType
Electronic
pubmed:day
5
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5705-14
pubmed:dateRevised
2011-11-7
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
The first global screening of protein substrates bearing protein-bound 3,4-Dihydroxyphenylalanine in Escherichia coli and human mitochondria.
pubmed:affiliation
Ben May Department for Cancer Research, University of Chicago, Chicago, IL 60637, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural