Abstract:
:While O(2)-binding hemoglobin-like proteins are present in many insects, prominent amounts of hemoglobin have only been found in a few species. Backswimmers of the genera Anisops and Buenoa (Notonectidae) have high concentrations of hemoglobin in the large tracheal cells of the abdomen. Oxygen from the hemoglobin is delivered to a gas bubble and controls the buoyant density, which enables the bugs to maintain their position without swimming and to remain stationary in the mid-water zone where they hunt for prey. We have obtained the cDNA sequences of three Anisops deanei hemoglobin chains by RT-PCR and RACE techniques. The deduced amino acid sequences show an unusual insertion of a single amino acid in the conserved helix E, but this does not affect protein stability or ligand binding kinetics. Recombinant A. deanei hemoglobin has an oxygen affinity of P(50) = 2.4 kPa (18 torr) and reveals the presence of a dimeric fraction or two different conformations. The absorption spectra demonstrate that the Anisops hemoglobin is a typical pentacoordinate globin. Phylogenetic analyses show that the backswimmer hemoglobins evolved within Heteroptera and most likely originated from an intracellular hemoglobin with divergent function.
journal_name
Insect Biochem Mol Bioljournal_title
Insect biochemistry and molecular biologyauthors
Wawrowski A,Matthews PG,Gleixner E,Kiger L,Marden MC,Hankeln T,Burmester Tdoi
10.1016/j.ibmb.2012.04.007subject
Has Abstractpub_date
2012-09-01 00:00:00pages
603-9issue
9eissn
0965-1748issn
1879-0240pii
S0965-1748(12)00062-8journal_volume
42pub_type
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