The Quorum-Sensing Hybrid Histidine Kinase LuxN of Vibrio harveyi Contains a Periplasmically Located N Terminus | Zendy

Kirsten Jung | Zendy; Tina Odenbach | Zendy; Melanie Timmen | Zendy

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The Quorum-Sensing Hybrid Histidine Kinase LuxN of Vibrio harveyi Contains a Periplasmically Located N Terminus

Author(s) -

Kirsten Jung,

Tina Odenbach,

Melanie Timmen

Publication year - 2007

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.01723-06

Subject(s) - periplasmic space , biology , histidine kinase , vibrio harveyi , biochemistry , histidine , transmembrane protein , peptide sequence , complementation , escherichia coli , autophosphorylation , mutant , amino acid , vibrio , kinase , protein kinase a , bacteria , genetics , gene , receptor

Hydropathy profile analyses of the amino acid sequence of the quorum-sensing hybrid histidine kinase LuxN of Vibrio harveyi predict a periplasmic location of the N terminus. To test this, two-hybrid proteins consisting of LuxN and an N-terminally fused maltose-binding protein with or without a leader sequence were analyzed with regard to the enzymatic activities of LuxN, protease accessibility, and complementation of an Escherichia coli malE mutant. The results strongly support a periplasmic location of the N terminus, implying that LuxN is anchored with nine transmembrane domains in the cytoplasmic membrane.

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