Characterization of Drosophila hemoglobin. Evidence for hemoglobin-mediated respiration in insects

In contrast to previous assumptions, the fruit fly Drosophila melanogaster possesses hemoglobin. This respiratory protein forms a monomer of about 17 kDa that is not exported into the hemolymph. Recombinant Drosophila hemoglobin displays a typical hexacoordinated deoxy spectrum and binds oxygen with...

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Bibliographic Details
Published in:The Journal of biological chemistry 2002-08, Vol.277 (32), p.29012-29017
Main Authors: Hankeln, Thomas, Jaenicke, Viviane, Kiger, Laurent, Dewilde, Sylvia, Ungerechts, Guy, Schmidt, Marc, Urban, Joachim, Marden, Michael C, Moens, Luc, Burmester, Thorsten
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Blotting, Western
Cloning, Molecular
Diffusion
Drosophila - genetics
Drosophila - metabolism
Hemoglobins - chemistry
In Situ Hybridization
Kinetics
Ligands
Models, Genetic
Oxygen - metabolism
Protein Binding
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Respiration
Reverse Transcriptase Polymerase Chain Reaction
RNA - metabolism
RNA, Messenger - metabolism
Signal Transduction
Time Factors
Transcription Factors
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Summary:In contrast to previous assumptions, the fruit fly Drosophila melanogaster possesses hemoglobin. This respiratory protein forms a monomer of about 17 kDa that is not exported into the hemolymph. Recombinant Drosophila hemoglobin displays a typical hexacoordinated deoxy spectrum and binds oxygen with an affinity of 0.12 torr. Four different hemoglobin transcripts have been identified, which are generated by two distinct promoters of the hemoglobin (glob1) gene but are identical in their coding regions. Putative binding sites for hypoxia-regulated transcription factors have been identified in the gene. Hemoglobin synthesis in Drosophila is mainly associated with the tracheal system and the fat body. This suggests that oxygen supply in insects may be more complex than thought previously and may depend on hemoglobin-mediated oxygen transport and storage in addition to simple diffusion.
ISSN:0021-9258
DOI:10.1074/jbc.M204009200