Linked Life Data

20209535

Source:http://linkedlifedata.com/resource/pubmed/id/20209535

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
2010-4-14
pubmed:abstractText
Protein splicing is a unique post-translational process in which an intein excises itself from a precursor with the concomitant ligation of flanking sequences. The binding of zinc to intein inhibits protein splicing reversibly and EDTA relieves the inhibition. Copper was found to inhibit protein trans splicing; however, the recovery of intein splicing required both EDTA and TCEP, suggesting a different inhibition mechanism for copper compared to zinc. In this work, we have investigated the binding properties and inhibition effects of copper ions on the RecA intein from Mycobacterium tuberculosis. Both Cu(+) and Cu(2+) exhibited high binding affinity to inteins, while different binding sites were identified. Cu(2+) coordinates to Cys1, the key residue involved in the mechanism of protein splicing, however, Cu(+) does not coordinate to cysteine. An in vitro inhibition assay indicated that monovalent Cu(+) demonstrates reversible inhibition to protein splicing, and the inhibitory efficiency is comparable to Zn(2+). Redox reaction between Cu(2+) and cysteine in inteins were observed and the rate constants were determined. The results suggested a dual role for Cu(2+) in the inhibition of intein splicing: strong coordination of Cu(2+) to key residues (including Cys1) in the intein, and subsequent oxidation of Cys1, the residue required for the N-->S acyl shift step in protein splicing. A kinetic study suggested that the coordination could be the major cause of inhibition effect of Cu(2+) initially, whereas the redox reaction could play an additional role in inhibition at a later stage.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1521-3765
pubmed:author
pubmed:issnType
Electronic
pubmed:day
12
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4297-306
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Binding and inhibition of copper ions to RecA inteins from Mycobacterium tuberculosis.
pubmed:affiliation
Department of Chemistry, CAS Key Laboratory of Soft Matter Chemistry, University of Science and Technology of China, 230026 Hefei, Anhui, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't