Λεπτομέρειες βιβλιογραφικής εγγραφής
| Τίτλος: |
Analysis of a Soluble (UreD:UreF:UreG) Accessory Protein Complex and Its Interactions with Klebsiella aerogenes Urease by Mass Spectrometry. |
| Συγγραφείς: |
Farrugia, Mark1, Han, Linjie2, Zhong, Yueyang2, Boer, Jodi, Ruotolo, Brandon2 bruotolo@umich.edu, Hausinger, Robert hausinge@msu.edu |
| Πηγή: |
Journal of the American Society for Mass Spectrometry. Sep2013, Vol. 24 Issue 9, p1328-1337. 10p. |
| Θεματικοί όροι: |
*Klebsiella, *Urease genetics, *Mass spectrometry, *Developmental biology, *Maltose, *Maltose-binding proteins |
| Περίληψη: |
Maturation of the nickel-containing urease of Klebsiella aerogenes is facilitated by the UreD, UreF, and UreG accessory proteins along with the UreE metallo-chaperone. A fusion of the maltose binding protein and UreD (MBP-UreD) was co-isolated with UreF and UreG in a soluble complex possessing a (MBP-UreD:UreF:UreG) quaternary structure. Within this complex a UreF:UreF interaction was identified by chemical cross-linking of the amino termini of its two UreF protomers, as shown by mass spectrometry of tryptic peptides. A pre-activation complex was formed by the interaction of (MBP-UreD:UreF:UreG) and urease. Mass spectrometry of intact protein species revealed a pathway for synthesis of the urease pre-activation complex in which individual hetero-trimer units of the (MBP-UreD:UreF:UreG) complex bind to urease. Together, these data provide important new insights into the structures of protein complexes associated with urease activation. [Figure not available: see fulltext.] [ABSTRACT FROM AUTHOR] |
| Βάση Δεδομένων: |
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