Cloning and characterization of a cDNA encoding a male-specific serum protein of the Mediterranean fruit fly,Ceratitis capitata, with sequence similarity to odourant-binding proteins

1998 ◽  
Vol 7 (4) ◽  
pp. 345-353 ◽  
Author(s):  
S. Thymlanou ◽  
M. Mavroidis ◽  
G. Kokolakis ◽  
K. Komitopoulou ◽  
A. Zacharopoulou ◽  
...  
2015 ◽  
Vol 126 ◽  
pp. 71-77 ◽  
Author(s):  
Luca Ruiu ◽  
Giovanni Falchi ◽  
Ignazio Floris ◽  
Maria Giovanna Marche ◽  
Maria Elena Mura ◽  
...  

1999 ◽  
Vol 265 (2) ◽  
pp. 798-808 ◽  
Author(s):  
Meletis Verras ◽  
Manolis Mavroidis ◽  
Giorgos Kokolakis ◽  
Polyxeni Gourzi ◽  
Antigone Zacharopoulou ◽  
...  

Genetics ◽  
1991 ◽  
Vol 127 (4) ◽  
pp. 769-780
Author(s):  
M Rina ◽  
C Savakis

Abstract Four genes encoding the major egg yolk polypeptides of the Mediterranean fruit fly Ceratitis capitata, vitellogenins 1 and 2 (VG1 and VG2), were cloned, characterized and partially sequenced. The genes are located on the same region of chromosome 5 and are organized in pairs, each encoding the two polypeptides on opposite DNA strands. Restriction and nucleotide sequence analysis indicate that the gene pairs have arisen from an ancestral pair by a relatively recent duplication event. The transcribed part is very similar to that of the Drosophila melanogaster yolk protein genes Yp1, Yp2 and Yp3. The Vg1 genes have two introns at the same positions as those in D. melanogaster Yp3; the Vg2 genes have only one of the introns, as do D. melanogaster Yp1 and Yp2. Comparison of the five polypeptide sequences shows extensive homology, with 27% of the residues being invariable. The sequence similarity of the processed proteins extends in two regions separated by a nonconserved region of varying size. Secondary structure predictions suggest a highly conserved secondary structure pattern in the two regions, which probably correspond to structural and functional domains. The carboxy-end domain of the C. capitata proteins shows the same sequence similarities with triacyglycerol lipases that have been reported previously for the D. melanogaster yolk proteins. Analysis of codon usage shows significant differences between D. melanogaster and C. capitata vitellogenins with the latter exhibiting a less biased representation of synonymous codons.


2015 ◽  
Vol 202 (2) ◽  
pp. 131-146 ◽  
Author(s):  
Paolo Solari ◽  
Valentina Corda ◽  
Giorgia Sollai ◽  
Sabine Kreissl ◽  
C. Giovanni Galizia ◽  
...  

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