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PMID: 7568075 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Regulski M, Tully T

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.

MeSH Terms
Alternative Splicing Amino Acid Sequence Animals Calcium/pharmacology Calmodulin/pharmacology Conserved Sequence Drosophila/enzymology Mammals Molecular Sequence Data Neurons/enzymology Nitric Oxide Synthase/biosynthesis,chemistry,metabolism Rats Restriction Mapping Sequence Homology, Amino Acid Transcription, Genetic
Chemicals
Calmodulin Nitric Oxide Synthase Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Regulski M
Cold Spring Harbor Laboratory, NY 11724, USA.
Tully T
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1995-09-26
Pages
9072-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC40926
Subset
IM
Grants
NIGMS NIH HHS · GM13643 · United States
Databases
GENBANK
U25117
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