Tags

Type your tag names separated by a space and hit enter

Structural and functional characterization of the microtubule interacting and trafficking domains of two oomycete chitin synthases.
FEBS J. 2016 08; 283(16):3072-88.FJ

Abstract

Chitin synthases (Chs) are responsible for the synthesis of chitin, a key structural cell wall polysaccharide in many organisms. They are essential for growth in certain oomycete species, some of which are pathogenic to diverse higher organisms. Recently, a microtubule interacting and trafficking (MIT) domain, which is not found in any fungal Chs, has been identified in some oomycete Chs proteins. Based on experimental data relating to the binding specificity of other eukaryotic MIT domains, there was speculation that this domain may be involved in the intracellular trafficking of Chs proteins. However, there is currently no evidence for this or any other function for the MIT domain in these enzymes. To attempt to elucidate their function, MIT domains from two Chs enzymes from the oomycete Saprolegnia monoica were cloned, expressed, and characterized. Both were shown to interact strongly with the plasma membrane component, phosphatidic acid, and to have additional putative interactions with proteins thought to be involved in protein transport and localization. Aiding our understanding of these data, the structure of the first MIT domain from a carbohydrate-active enzyme (MIT1) was solved by NMR, and a model structure of a second MIT domain (MIT2) was built by homology modeling. Our results suggest a potential function for these MIT domains in the intracellular transport and/or regulation of Chs enzymes in the oomycetes.

DATABASE

Structural data are available in the Biological Magnetic Resonance Bank (BMRB) database under the accession number 19987 and the PDB database under the accession number 2MPK.

Authors+Show Affiliations

Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, Stockholm, Sweden.Department of Biochemistry and Biophysics, The Arrhenius Laboratory, Stockholm University, Sweden.Division of Theoretical Chemistry and Biology, School of Biotechnology, Royal Institute of Technology (KTH), Stockholm, Sweden.Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, Stockholm, Sweden.Department of Biochemistry and Biophysics, The Arrhenius Laboratory, Stockholm University, Sweden.Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, Stockholm, Sweden.Division of Theoretical Chemistry and Biology, School of Biotechnology, Royal Institute of Technology (KTH), Stockholm, Sweden.Department of Biochemistry and Biophysics, The Arrhenius Laboratory, Stockholm University, Sweden.Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, Stockholm, Sweden. ARC Centre of Excellence in Plant Cell Walls, School of Agriculture, Food and Wine, The University of Adelaide, Waite Campus, Urrbrae, South Australia, Australia.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

27363606

Citation

Brown, Christian, et al. "Structural and Functional Characterization of the Microtubule Interacting and Trafficking Domains of Two Oomycete Chitin Synthases." The FEBS Journal, vol. 283, no. 16, 2016, pp. 3072-88.
Brown C, Szpryngiel S, Kuang G, et al. Structural and functional characterization of the microtubule interacting and trafficking domains of two oomycete chitin synthases. FEBS J. 2016;283(16):3072-88.
Brown, C., Szpryngiel, S., Kuang, G., Srivastava, V., Ye, W., McKee, L. S., Tu, Y., Mäler, L., & Bulone, V. (2016). Structural and functional characterization of the microtubule interacting and trafficking domains of two oomycete chitin synthases. The FEBS Journal, 283(16), 3072-88. https://doi.org/10.1111/febs.13794
Brown C, et al. Structural and Functional Characterization of the Microtubule Interacting and Trafficking Domains of Two Oomycete Chitin Synthases. FEBS J. 2016;283(16):3072-88. PubMed PMID: 27363606.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural and functional characterization of the microtubule interacting and trafficking domains of two oomycete chitin synthases. AU - Brown,Christian, AU - Szpryngiel,Scarlett, AU - Kuang,Guanglin, AU - Srivastava,Vaibhav, AU - Ye,Weihua, AU - McKee,Lauren S, AU - Tu,Yaoquan, AU - Mäler,Lena, AU - Bulone,Vincent, Y1 - 2016/07/22/ PY - 2016/01/05/received PY - 2016/05/31/revised PY - 2016/06/28/accepted PY - 2016/7/2/entrez PY - 2016/7/2/pubmed PY - 2017/6/16/medline KW - NMR structure KW - chitin synthase KW - microtubule interacting and trafficking domain KW - oomycete KW - phospholipids SP - 3072 EP - 88 JF - The FEBS journal JO - FEBS J. VL - 283 IS - 16 N2 - UNLABELLED: Chitin synthases (Chs) are responsible for the synthesis of chitin, a key structural cell wall polysaccharide in many organisms. They are essential for growth in certain oomycete species, some of which are pathogenic to diverse higher organisms. Recently, a microtubule interacting and trafficking (MIT) domain, which is not found in any fungal Chs, has been identified in some oomycete Chs proteins. Based on experimental data relating to the binding specificity of other eukaryotic MIT domains, there was speculation that this domain may be involved in the intracellular trafficking of Chs proteins. However, there is currently no evidence for this or any other function for the MIT domain in these enzymes. To attempt to elucidate their function, MIT domains from two Chs enzymes from the oomycete Saprolegnia monoica were cloned, expressed, and characterized. Both were shown to interact strongly with the plasma membrane component, phosphatidic acid, and to have additional putative interactions with proteins thought to be involved in protein transport and localization. Aiding our understanding of these data, the structure of the first MIT domain from a carbohydrate-active enzyme (MIT1) was solved by NMR, and a model structure of a second MIT domain (MIT2) was built by homology modeling. Our results suggest a potential function for these MIT domains in the intracellular transport and/or regulation of Chs enzymes in the oomycetes. DATABASE: Structural data are available in the Biological Magnetic Resonance Bank (BMRB) database under the accession number 19987 and the PDB database under the accession number 2MPK. SN - 1742-4658 UR - https://www.unboundmedicine.com/medline/citation/27363606/Structural_and_functional_characterization_of_the_microtubule_interacting_and_trafficking_domains_of_two_oomycete_chitin_synthases_ L2 - https://doi.org/10.1111/febs.13794 DB - PRIME DP - Unbound Medicine ER -