Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE1-34

Wael E. Houssen; Stephen H. Wright; Arnout P. Kalverda; Gary S. Thompson; Sharon M. Kelly; Marcel Jaspars

doi:10.1002/cbic.201000305

Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE1-34

ChemBioChem ◽

10.1002/cbic.201000305 ◽

2010 ◽

Vol 11 (13) ◽

pp. 1867-1873 ◽

Cited By ~ 20

Author(s):

Wael E. Houssen ◽

Stephen H. Wright ◽

Arnout P. Kalverda ◽

Gary S. Thompson ◽

Sharon M. Kelly ◽

...

Keyword(s):

Solution Structure ◽

Leader Sequence ◽

Precursor Peptide

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Enzymatic Cyclization of a Potent Bowman-Birk Protease Inhibitor, Sunflower Trypsin Inhibitor-1, and Solution Structure of an Acyclic Precursor Peptide

Journal of Biological Chemistry ◽

10.1074/jbc.m212996200 ◽

2003 ◽

Vol 278 (24) ◽

pp. 21782-21789 ◽

Cited By ~ 58

Author(s):

Ute C. Marx ◽

Michael L. J. Korsinczky ◽

Horst Joachim Schirra ◽

Alun Jones ◽

Barrie Condie ◽

...

Keyword(s):

Protease Inhibitor ◽

Trypsin Inhibitor ◽

Solution Structure ◽

Precursor Peptide ◽

Acyclic Precursor

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Distinct Contributions of the Nisin Biosynthesis Enzymes NisB and NisC and Transporter NisT to Prenisin Production by Lactococcus lactis

Applied and Environmental Microbiology ◽

10.1128/aem.00342-08 ◽

2008 ◽

Vol 74 (17) ◽

pp. 5541-5548 ◽

Cited By ~ 26

Author(s):

H. Bart van den Berg van Saparoea ◽

Patrick J. Bakkes ◽

Gert N. Moll ◽

Arnold J. M. Driessen

Keyword(s):

Growth Rate ◽

Kinetic Analysis ◽

Lactococcus Lactis ◽

Leader Sequence ◽

Intracellular Accumulation ◽

Nisin Production ◽

Precursor Peptide ◽

In Cells

ABSTRACT Several Lactococcus lactis strains produce the lantibiotic nisin. The dedicated enzymes NisB and NisC and the transporter NisT modify and secrete the ribosomally synthesized nisin precursor peptide. NisB can function in the absence of the cyclase NisC, yielding the dehydrated prenisin that lacks the thioether rings. A kinetic analysis of nisin production by L. lactis NZ9700 demonstrated that the prenisin was released from the cell into the medium before the processing of the leader sequence occurred. Upon the deletion of nisC, the production of prenisin was reduced by 70%, while in the absence of nisB, the production of prenisin was nearly completely abolished. In cells lacking nisT, no secretion was observed, while the expression of nisABC in these cells resulted in considerable growth rate inhibition caused by the intracellular accumulation of active nisin. Overall, these data indicate that the efficiency of prenisin transport by NisT is markedly enhanced by NisB, suggesting a channeling mechanism of prenisin transfer between the nisin modification enzymes and the transporter.

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