期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 2, 页码 678-683出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1215033110
关键词
protein crystallization; sugar binding protein; sugar binding specificity; host recognition; ABC transporter
资金
- National Institutes of Health [GM54616, AI74866]
- Materials Research Science and Engineering Centers program of the National Science Foundation
- National Science Foundation [IOS-0818613, IOS11211019]
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [1121019] Funding Source: National Science Foundation
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [1120901] Funding Source: National Science Foundation
Agrobacterium tumefaciens is a broad host range plant pathogen that combinatorially recognizes diverse host molecules including phenolics, low pH, and aldose monosaccharides to activate its pathogenic pathways. Chromosomal virulence gene E (chvE) encodes a periplasmic-binding protein that binds several neutral sugars and sugar acids, and subsequently interacts with the VirA/VirG regulatory system to stimulate virulence (vir) gene expression. Here, a combination of genetics, X-ray crystallography, and isothermal calorimetry reveals how ChvE binds the different monosaccharides and also shows that binding of sugar acids is pH dependent. Moreover, the potency of a sugar for vir gene expression is modulated by a transport system that also relies on ChvE. These two circuits tune the overall system to respond to sugar concentrations encountered in vivo. Finally, using chvE mutants with restricted sugar specificities, we show that there is host variation in regard to the types of sugars that are limiting for vir induction.
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