Silencing of Glutamine: Fructose-6-Phosphate Aminotransferase Impairs Growth and Development in Sogatella furcifera (Hemiptera: Delphacidae)

Bibliographic Details
Title: Silencing of Glutamine: Fructose-6-Phosphate Aminotransferase Impairs Growth and Development in Sogatella furcifera (Hemiptera: Delphacidae)
Authors: Zhao Wang, Guiyun Long, Huan Zhu, Daochao Jin, Hong Yang, Cao Zhou
Source: Biomolecules, Vol 13, Iss 10, p 1433 (2023)
Publisher Information: MDPI AG, 2023.
Publication Year: 2023
Collection: LCC:Microbiology
Subject Terms: glutamine: fructose-6-phosphate aminotransferase, gene expression, RNA interference, Sogatella furcifera, Microbiology, QR1-502
More Details: Glutamine: fructose-6-phosphate aminotransferase (GFAT), the fourth enzyme in the chitin synthesis pathway, exerts wide-ranging effects on the growth and development of organisms. However, the role of GFAT in Sogatella furcifera remains unknown. In this study, the functional significance of the GFAT gene of S. furcifera was analyzed using a reverse transcription-polymerase chain reaction and RNA interference (RNAi) analyses. The complementary DNA sequence of SfGFAT was 3162 bp in length and contained a 2067 bp open reading frame encoding 688 amino acid residues. Structural domain analysis indicated that the SfGFAT protein consisted of one glutamine aminotransferase class 2 domain and two sugar isomerase domains. Expression profile analysis revealed that SfGFAT was expressed throughout the egg, nymph, and adult phases and was strongly expressed on the first day of each nymph stage and in the integuments of five tissues. RNAi results revealed that SfGFAT gene silencing significantly inhibited the mRNA expression of the target gene and resulted in severe mortality among S. furcifera. In summary, these findings demonstrate that SfGFAT plays a critical role in the development of S. furcifera. Moreover, these results may aid in the development of methods to control the spread of S. furcifera.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2218-273X
Relation: https://www.mdpi.com/2218-273X/13/10/1433; https://doaj.org/toc/2218-273X
DOI: 10.3390/biom13101433
Access URL: https://doaj.org/article/19deb24d5c6d42168e819f599bcc72b1
Accession Number: edsdoj.19deb24d5c6d42168e819f599bcc72b1
Database: Directory of Open Access Journals
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More Details
ISSN:2218273X
DOI:10.3390/biom13101433
Published in:Biomolecules
Language:English