Characterization of the hemoglobin of the backswimmer Anisops deanei (Hemiptera).

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.

authors

Wawrowski A,Matthews PG,Gleixner E,Kiger L,Marden MC,Hankeln T,Burmester T

doi

10.1016/j.ibmb.2012.04.007

subject

Has Abstract

pub_date

2012-09-01 00:00:00

pages

603-9

issue

9

eissn

0965-1748

issn

1879-0240

pii

S0965-1748(12)00062-8

journal_volume

42

pub_type

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