Use this url to cite publication: https://hdl.handle.net/20.500.12259/48878
Options
Cloning and expression of transmembrane domain segments of Arabidopsis thaliana RBOH D enzyme
Type of publication
Tezės kitame recenzuojamame leidinyje / Theses in other peer-reviewed publication (T1e)
Author(s)
Druceikaitė, Kristina | Lietuvos agrarinių ir miškų mokslų centro filialas Sodininkystės ir daržininkystės institutas |
Baniulis, Danas | Lietuvos agrarinių ir miškų mokslų centro filialas Sodininkystės ir daržininkystės institutas |
Title
Cloning and expression of transmembrane domain segments of Arabidopsis thaliana RBOH D enzyme
Is part of
The vital nature sign [elektroninis išteklius] : 9th international scientific conference : abstract book. Kaunas : Vytautas Magnus university, 2015, [no. 9]
Date Issued
Date Issued |
---|
2015 |
Publisher
Kaunas : Vytautas Magnus university
Extent
p. 71-71
Field of Science
Abstract
Production of reactive oxygen species (ROS) is important cell signaling component involved in plant response to stress. NADPH-oxidase, also known as respiratory burst oxidase homologue (RBOH) in plants, is a superoxide producing NOX family protein that is located in plasma membrane and contributes to ROS generation outside the plasma membrane in the apoplast. A. thaliana has ten RBOH genes (RBOH A-J). RBOH D is expressed in all plant tissues and takes part in regulation of response to pathogen and abiotic stress. Plant RBOH proteins show unique structural and regulation features that include calcium binding and different cytosolic component role in regulation of the enzyme activity. Meanwhile, structure of small N-terminal cytosolic domain of plant RBOH was studied so far, further structural and functional studies of plant RBOH homologues could help to understand the role of these enzymes in cell signaling. Heterologous expression and purification of transmembrane proteins is challenging due to their hydrophobic membrane domain. However, valuable information about transmembrane protein structure and function may be obtained by expression and characterization of separate membrane domain fragments. Aim of this study was to identify, clone and optimize the production of segments of A. thaliana RBOH D protein membrane domain in E. coli expression system. To identify transmembrane domain of RBOH D, bioinformatics analysis of amino acid sequence hydrophobicity profile, transmembrane protein domain modeling and assessment of previously predicted structures of other NOX family proteins, such as NOX2, was used. Six transmembrane helices were identified and the third and fifth helices each contained two conserved His residues, which are considered to coordinate the two hemes involved in superoxide production. [...].
Type of document
type::text::conference output::conference proceedings::conference paper
Language
Anglų / English (en)
Coverage Spatial
Lietuva / Lithuania (LT)