HrpZ Family
   HOME

TheInfoList



OR:

The ''Pseudomonas syringae'' HrpZ Cation Channel (HrpZ) Family
TC# 1.C.56
is a member of the RTX-toxin superfamily. The Harpin-PSS (HrpZ
TC# 1.C.56.1.1
protein is secreted by '' Pseudomonas syringae'' via the Hrp secretion system (IIISP
TC# 3.A.6
and elicits a hypersensitive response (HR) in non-host plants upon infection and pathogenicity in hosts. It contains several repetitive regions and exhibits two extended (20 residue) regions of moderate hydrophobicity that might serve as α-helical TMSs. The HrpZ cation channel is predicted to be largely of α-structure. HrpZ - a harpin - is a highly thermostable protein that exhibits multifunctional abilities, e.g., it elicits the hypersensitive response (HR), enhances plant growth, acts as a virulence factor, and forms pores in plant plasma membranes as well as artificial membranes. Homologues are not found in organisms other than '' P. syringae''.


Function

When inserted into liposomes and synthetic bilayers at low concentrations (2 nM), it provokes a cation-selective ion current with large unitary conductance. Chloride is not transported. It has been hypothesized that such channels could allow nutrient release and/or delivery of virulence factors during bacterial colonization of host plants. The leucine-zipper-like motifs may take part in the formation of oligomeric aggregates, and oligomerization could be related to HR elicitation.


Transport reaction

The generalized transport reaction thought to be catalyzed by HrpZ is: :Small molecules (in) → Small molecules (out)


References


Further reading

*{{cite journal , last1 = Chen , first1 = Jonathan S. , last2 = Reddy , first2 = Vamsee , last3 = Chen , first3 = Joshua H. , last4 = Shlykov , first4 = Maksim A. , last5 = Zheng , first5 = Wei Hao , last6 = Cho , first6 = Jaehoon , last7 = Yen , first7 = Ming Ren , last8 = Saier , first8 = Milton H. , year = 2011 , title = Phylogenetic characterization of transport protein superfamilies: superiority of SuperfamilyTree programs over those based on multiple alignments , journal = Journal of Molecular Microbiology and Biotechnology , volume = 21 , issue = 3–4, pages = 83–96 , doi = 10.1159/000334611 , pmid = 22286036 , pmc = 3290041 Bacterial toxins