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THE KNICKKOPF DOMON DOMAIN IS ESSENTIAL FOR CUTICLE DIFFERENTIATION IN Drosophila melanogaster
Author(s) -
Shaik Khaleelulla Saheb,
Wang Yiwen,
Aravind L.,
Moussian Bernard
Publication year - 2014
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21165
Subject(s) - drosophila melanogaster , biology , melanogaster , biochemistry , histidine , amino acid , extracellular , mutant , arginine , methionine , lysine , tryptophan , heme , function (biology) , microbiology and biotechnology , gene , enzyme
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.