Molecular and biochemical characterization of dNOS: a Drosophila Ca2+/calmodulin-dependent nitric oxide synthase

Regulski, M., Tully, T. (September 1995) Molecular and biochemical characterization of dNOS: a Drosophila Ca2+/calmodulin-dependent nitric oxide synthase. Proc Natl Acad Sci U S A, 92 (20). pp. 9072-6. ISSN 0027-8424 (Print)

[thumbnail of Paper]
Preview
PDF (Paper)
Tully PNAS 1995.pdf - Published Version

Download (1MB) | Preview

Abstract

Nitric oxide (NO) is an intercellular messenger involved with various aspects of mammalian physiology ranging from vasodilation and macrophage cytotoxicity to neuronal transmission. NO is synthesized from L-arginine by NO synthase (NOS). Here, we report the cloning of a Drosophila NOS gene, dNOS, located at cytological position 32B. The dNOS cDNA encodes a protein of 152 kDa, with 43% amino acid sequence identity to rat neuronal NOS. Like mammalian NOSs, DNOS protein contains putative binding sites for calmodulin, FMN, FAD, and NADPH. DNOS activity is Ca2+/calmodulin dependent when expressed in cell culture. An alternative RNA splicing pattern also exists for dNOS, which is identical to that for vertebrate neuronal NOS. These structural and functional observations demonstrate remarkable conservation of NOS between vertebrates and invertebrates.

Item Type: Paper
Uncontrolled Keywords: Alternative Splicing Amino Acid Sequence Animals Calcium/pharmacology Calmodulin/pharmacology Comparative Study Conserved Sequence Drosophila/ enzymology Mammals Molecular Sequence Data Neurons/enzymology Nitric Oxide Synthase/ biosynthesis/ chemistry/metabolism Rats Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Restriction Mapping Sequence Homology, Amino Acid Transcription, Genetic
Subjects: bioinformatics > genomics and proteomics > design > amino acid design
organism description > animal > insect > Drosophila
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > nitric oxide synthase
organism description > animal > mammal > rodent > rat
organism description > animal > mammal > rodent > rat
CSHL Authors:
Communities: CSHL labs > Tully lab
Depositing User: Jessica Koos
Date: 26 September 1995
Date Deposited: 08 Aug 2014 20:53
Last Modified: 09 Nov 2017 19:27
PMCID: PMC40926
Related URLs:
URI: https://repository.cshl.edu/id/eprint/30637

Actions (login required)

Administrator's edit/view item Administrator's edit/view item