Abstract

Transmembrane channel-like (TMC) genes encode a family of evolutionarily conserved membrane proteins. Mutations in the TMC1 and TMC2 cause deafness in humans and mice. However, their functions in insects are is still not well known. Here we cloned three tmc genes, Nltmc3, Nltmc5, and Nltmc7 from brown planthoppers. The predicted amino acid sequences showed high identity with other species homologs and have the characteristic eight or nine transmembrane domains and TMC domain architecture. We detected these three genes in all developmental stages and examined tissues. Interestingly, we found Nltmc3 was highly expressed in the female reproductive organ especially in the oviduct. RNAi-mediated silencing of Nltmc3 substantially decreased the egg-laying number and impaired ovary development. Our results indicate that Nltmc3 has an essential role in the ovary development of brown planthoppers.

Highlights

  • Exon-intron organization was analyzed by comparing cloned cDNAs and the corresponding genomic sequence, revealing that Nltmc3 is located on scaffold 754 and scaffold 3202, Nltmc5 is located on scaffold 943, and Nltmc7 is located on scaffold 2298 (Figure 1)

  • Eight Transmembrane channel-like (TMC) proteins can be grouped into three subfamilies A, B, and C, based on sequence homology (Keresztes et al, 2003)

  • Phylogenetic tree comparison showed that NlTMC3 clustered with MmTMC1, MmTMC2, MmMTC3, CeTMC1, CeTMC2, and DmTMC, which belongs to A subfamily

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Summary

Introduction

Transmembrane channel-like (TMC) proteins have been identified from insects to mammals (Keresztes et al, 2003; Kurima et al, 2003; Guo et al, 2016). Eight TMC proteins were presented in vertebrates including humans and mice (Keresztes et al, 2003; Kurima et al, 2003). They can be grouped into three subfamilies A, B, and C, in terms of their sequence homology and similarities of the genomic structures of their respective genes (Keresztes et al, 2003). All tmc genes are strongly predicted to encode proteins with at least six transmembrane domains and a novel conserved CWETXVGQEly(K/R)LtvXD amino-acid sequence motif that termed as TMC domain (Keresztes et al, 2003; Kurima et al, 2003)

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