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Shaik, Khaleelulla Saheb and Wang, Yiwen and Aravind, L and Moussian, Bernard (2014) THE KNICKKOPF DOMON DOMAIN IS ESSENTIAL FOR CUTICLE DIFFERENTIATION IN Drosophila melanogaster. In: ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY, 86 (2). pp. 100-106.

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Official URL: http://dx.doi.org/10.1002/arch.21165


The dopamine monoxygenase N-terminal (DOMON) domain is found in extracellular proteins across several eukaryotic and prokaryotic taxa. It has been proposed that this domain binds to heme or sugar moieties. Here, we have analyzed the role of four highly conserved amino acids in the DOMON domain of the Drosophila melanogaster Knickkopf protein that is inserted into the apical plasma membrane and assists extracellular chitin organization. In principal, we generated Knickkopf versions with exchanged residues tryptophan(299,) methionine(333), arginine(401), or histidine(437), and scored for the ability of the respective engineered protein to normalize the knickkopf mutant phenotype. Our results confirm the absolute necessity of tryptophan(299,) methionine(333), and histidine(437) for Knickkopf function and stability, the latter two being predicted to be critical for heme binding. In contrast, arginine(401) is required for full efficiency of Knickkopf activity. Taken together, our genetic data support the prediction of these residues to mediate the function of Knickkopf during cuticle differentiation in insects. Hence, the DOMON domain is apparently an essential factor contributing to the construction of polysaccharide-based extracellular matrices.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to the WILEY-BLACKWELL, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
Keywords: Drosophila; chitin; redox reaction; cuticle; DOMON
Department/Centre: Division of Biological Sciences > Molecular Reproduction, Development & Genetics
Depositing User: Id for Latest eprints
Date Deposited: 24 Jun 2014 05:15
Last Modified: 24 Jun 2014 05:15
URI: http://eprints.iisc.ac.in/id/eprint/49291

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