| Autor: |
Zakharkin SO; Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock 72205, USA., Gordadze AV, Korochkina SE, Mathiopoulos KD, Della Torre A, Benes H |
| Jazyk: |
angličtina |
| Zdroj: |
European journal of biochemistry [Eur J Biochem] 1997 Jun 15; Vol. 246 (3), pp. 719-26. |
| DOI: |
10.1111/j.1432-1033.1997.t01-1-00719.x |
| Abstrakt: |
During the last larval instar, dipteran insects synthesize two hexamerins rich in aromatic residues, typified by the larval serum proteins 1 and 2 (LSP-1 and LSP-2) of Drosophila melanogaster. We report here the characterization of a complete cDNA sequence encoding a LSP-1-like protein from a lower dipteran insect, the malaria mosquito Anopheles gambiae. The cDNA encodes the subunit of a homohexamer, A. gambiae hexamerin-1.1 (AgHex-1.1), which is a major pupal protein but only a minor constituent of late larval hemolymph. AgHex-1.1 is moderately rich in methionine (3.9%) and particularly rich in aromatic residues (21% Phe+Tyr). Cytogenetic analysis reveals AgHex-1.1 to be encoded by a single-copy gene localized to division 22F within the proximal 2La inversion breakpoint of chromosome 2 of A. gambiae. The AgHex-1.1 transcript is first detected in fourth-instar larvae (L4) and disappears abruptly in early pupae. In situ hybridization shows accumulation of the transcript uniquely in the larval fat body. AgHex-1.1 mRNA is re-expressed in male and female adults at about 10% of the L4 level, with no effect of bloodfeeding in females. The potential roles of AgHex-1.1 in Anopheles development and reproductive maturation are discussed. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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