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Tyrosine hydroxylase is crucial for pupal pigmentation in Zeugodacus tau (Walker) (Diptera: Tephritidae).

Authors :
Zhang HH
Zhang QW
Idrees A
Lin J
Song XS
Ji QE
Du YG
Zheng ML
Chen JH
Source :
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology [Comp Biochem Physiol B Biochem Mol Biol] 2019 May; Vol. 231, pp. 11-19. Date of Electronic Publication: 2019 Feb 05.
Publication Year :
2019

Abstract

Tyrosine hydroxylase (TH) is the initial enzyme responsible for cuticle sclerotization and pigmentation in many insect species, but to date, no direct functional studies have focused on TH in Zeugodacus tau. Here, the 3336-bp full-length cDNA of TH was isolated from Z. tau, a notorious horticultural pest infesting fruits and vegetables. qRT-polymerase chain reaction revealed that ZtTH transcripts were highly abundant at the time of pupal tanning and during adult emergence and were expressed in the midgut, integument and head of molting larvae. The pupation and eclosion rates gradually decreased when the 1st-instar larvae were fed diets containing higher concentrations of the TH inhibitor 3-iodo-tyrosine (3-IT). Moreover, pupal weights were significantly decreased, and abnormal uncolored phenotypes were observed after 20 mg/g 3-IT was incorporated into the diet. In addition, the suppression of TH function (mediated by RNA interference) led to a decrease in TH mRNAs and eclosion rates, accompanied by less-pigmented phenotypes. There was a severe impairment of larval-pupal cuticle tanning, leading to pupae with less yellowish pigment or that were completely white and transparent, when we injected 2 μL of 24.4 mM or 73.27 mM 3-IT into 3rd-instar larvae or prepupae. These results suggest that TH is an important enzyme for the normal growth and pupal pigmentation of Z. tau and that TH is a potential gene target for use in the control of Z. tau.<br /> (Copyright © 2019 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1879-1107
Volume :
231
Database :
MEDLINE
Journal :
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
Publication Type :
Academic Journal
Accession number :
30735775
Full Text :
https://doi.org/10.1016/j.cbpb.2019.01.017