Mutations of an Arylalkylamine-N-acetyltransferase, Bm-iAANAT, Are Responsible for Silkworm Melanism Mutant

Dai, Fangyin; Qiao, Liang; Tong, Xiaoling; Cao, Chunyan; Chen, Peng; Chen, Jun; Lü, Cheng; Zhang, Xiang

doi:10.1074/jbc.m109.096743

Cited by 89 publications

(78 citation statements)

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“…Mapping of stony locus and bioinformatic analysis of candidate regions were performed, as described previously (Dai et al 2010). In Bm_nscaf2827 (chromosome 8), we identified polymorphic PCR markers between the parents, Dazao-stony and C108, and assessed these in BC 1 F individuals.…”

Section: Positional Cloningmentioning

confidence: 99%

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Mutation of a Cuticular Protein,BmorCPR2, Alters Larval Body Shape and Adaptability in Silkworm,Bombyx mori

et al. 2014

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Cuticular proteins (CPs) are crucial components of the insect cuticle. Although numerous genes encoding cuticular proteins have been identified in known insect genomes to date, their functions in maintaining insect body shape and adaptability remain largely unknown. In the current study, positional cloning led to the identification of a gene encoding an RR1-type cuticular protein, BmorCPR2, highly expressed in larval chitin-rich tissues and at the mulberry leaf-eating stages, which is responsible for the silkworm stony mutant. In the Dazao-stony strain, the BmorCPR2 allele is a deletion mutation with significantly lower expression, compared to the wild-type Dazao strain. Dysfunctional BmorCPR2 in the stony mutant lost chitin binding ability, leading to reduced chitin content in larval cuticle, limitation of cuticle extension, abatement of cuticle tensile properties, and aberrant ratio between internodes and intersegmental folds. These variations induce a significant decrease in cuticle capacity to hold the growing internal organs in the larval development process, resulting in whole-body stiffness, tightness, and hardness, bulging intersegmental folds, and serious defects in larval adaptability. To our knowledge, this is the first study to report the corresponding phenotype of stony in insects caused by mutation of RR1-type cuticular protein. Our findings collectively shed light on the specific role of cuticular proteins in maintaining normal larval body shape and will aid in the development of pest control strategies for the management of Lepidoptera.T HE cuticle covering the entire body surface of insects not only participates in defense against pathogens and adverse environmental factors, but is also indispensable for constructing and maintaining external morphological characteristics and locomotion during the entire developmental process (Wigglesworth 1957;Delon and Payre 2004;Moussian et al. 2005). Therefore, the cuticle greatly enhances survival ability and adaptability of insects, ensuring its continued existence as one of the most successful life forms in the animal kingdom.The cuticle is a complex composite material mainly comprising chitin fibers and proteins (Andersen et al. 1995;Moussian 2010). Chitin is the polymer of b-1,4-linked N-acetyl-D-glucosamine (Gilbert 2011, Chap. 7). In procuticles, chitin fibers are arranged in laminae in an antiparallel manner and superimpose each other, forming sheets of fibrils that are stacked in a helicoidal fashion, maintaining cuticle structure, elasticity, and stability (Bouligand 1965;Neville and Luke 1969;Moussian 2010). In terrestrial insects, the chitin content is positively correlated with body size, suggesting a close relationship with cuticle extension and expansion (Merzendorfer and Zimoch 2003;Lease and Wolf 2010).Cuticular proteins (CPs), the principal structural constituents of cuticle, are encoded by more than 100 genes in known insect genomes (Andersen et al. 1995 The soft, flexible cuticle of Lepidoptera larvae not only bears pressure from ...

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Section: Positional Cloningmentioning

confidence: 99%

“…Quantitative RT-PCR was performed as described previously (Dai et al 2010), using the StepOneTM real-time PCR xystem (ABI). Primers used for qRT-PCR are listed in Table S1.…”

Section: Quantitative Rt-pcrmentioning

confidence: 99%

Mutation of a Cuticular Protein,BmorCPR2, Alters Larval Body Shape and Adaptability in Silkworm,Bombyx mori

et al. 2014

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“…EU378921, KF246473-KF246476, KF290562, BK008791, and BK008792). The AANAT family that is the subject of the current report is distinct from another family also named AANAT, which includes enzymes involved in acetylation of dopamine and other arylalkylamines in insects (11,12). These two protein families are only distantly related to each other, although both belong to the GCN5 superfamily of acetyltransferases.…”

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confidence: 94%

Drastic neofunctionalization associated with evolution of the timezyme AANAT 500 Mya

Falcón

Coon

Besseau

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Melatonin (N-acetyl-5-methoxytrypamine) is the vertebrate hormone of the night: circulating levels at night are markedly higher than day levels. This increase is driven by precisely regulated increases in acetylation of serotonin in the pineal gland by arylalkylamine N-acetyltransferase (AANAT), the penultimate enzyme in the synthesis of melatonin. This unique essential role of AANAT in vertebrate timekeeping is recognized by the moniker the timezyme. AANAT is also found in the retina, where melatonin is thought to play a paracrine role. Here, we focused on the evolution of AANAT in early vertebrates. AANATs from Agnathans (lamprey) and Chondrichthyes (catshark and elephant shark) were cloned, and it was found that pineal glands and retinas from these groups express a form of AANAT that is compositionally, biochemically, and kinetically similar to AANATs found in bony vertebrates (VT-AANAT). Examination of the available genomes indicates that VT-AANAT is absent from other forms of life, including the Cephalochordate amphioxus. Phylogenetic analysis and evolutionary rate estimation indicate that VT-AANAT evolved from the nonvertebrate form of AANAT after the Cephalochordate-Vertebrate split over one-half billion years ago. The emergence of VT-AANAT apparently involved a dramatic acceleration of evolution that accompanied neofunctionalization after a duplication of the nonvertebrate AANAT gene. This scenario is consistent with the hypotheses that the advent of VT-AANAT contributed to the evolution of the pineal gland and lateral eyes from a common ancestral photodetector and that it was not a posthoc recruitment.E yes have evolved in all animals to facilitate interactions with the photic environment (1, 2). However, among animals, vertebrates are unique in that they also possess a photoneuroendocrine structure, the pineal gland (3). It converts the 24-h rhythm in environmental lighting into a 24-h rhythm in circulating melatonin, thereby providing a unique and valuable signal of the photic environment. The details of pineal evolution are not clear (4, 5). However, it has been posited that an essential element was arylalkylamine N-acetyltransferase (AANAT; E.C. 2.3.1.87), the penultimate enzyme in the melatonin biosynthesis pathway (6-8); this scenario is referred to as the AANAT hypothesis of pineal evolution (7,8).AANAT catalyzes the N-acetylation of arylalkylamines using acetyl CoA (AcCoA) as the acetyl group donor. The AANAT family, which belongs to the GCN5 superfamily (9, 10), is composed of two subfamilies termed vertebrate (VT) AANAT and nonvertebrate (NV) AANAT. † This nomenclature reflects the phylogenetic distribution of the family members (13-17). The most striking differences between VT-and NV-AANAT are found in regulatory and catalytic regions of the encoded proteins (Fig. 1), consistent with different metabolic roles (7,8).The NV-AANAT is thought to perform a detoxification function through acetylation of a broad range of endogenous and exogenous arylalkylamines and polyamines (13-16). It has been fo...

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“…Recently, the mln mutant, which exhibits a readily distinguishable phenotype in both the larvae and adults, was characterised at the molecular level based on positional cloning and functional analysis (Dai et al, 2010;Zhan et al, 2010). Linkage analysis and genomic studies have shown that Bombyx arylalkamine-N-acetyl transferase, the homologous gene (Dat) that converts dopamine into N-acetyl dopamine, encodes a precursor of N-acetyl dopamine, sclerotin in Drosophila and it is the gene responsible for mln (Dai et al, 2010;Zhan et al, 2010). However, other causal genes have not yet been identified.…”

Section: Introductionmentioning

confidence: 99%

Mapping and recombination analysis of two moth colour mutations, Black moth and Wild wing spot, in the silkworm Bombyx mori

et al. 2015

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Many lepidopteran insects exhibit body colour variations, where the high phenotypic diversity observed in the wings and bodies of adults provides opportunities for studying adaptive morphological evolution. In the silkworm Bombyx mori, two genes responsible for moth colour mutation, Bm and Ws, have been mapped to 0.0 and 14.7 cM of the B. mori genetic linkage group 17; however, these genes have not been identified at the molecular level. We performed positional cloning of both genes to elucidate the molecular mechanisms that underlie the moth wing-and body-colour patterns in B. mori. We successfully narrowed down Bm and Ws to~2-Mb-long and 100-kb-long regions on the same scaffold Bm_scaf33. Gene prediction analysis of this region identified 77 candidate genes in the Bm region, whereas there were no candidate genes in the Ws region. Fluorescence in-situ hybridisation analysis in Bm mutant detected chromosome inversion, which explains why there are no recombination in the corresponding region. The comparative genomic analysis demonstrated that the candidate regions of both genes shared synteny with a region associated with wing-and body-colour variations in other lepidopteran species including Biston betularia and Heliconius butterflies. These results suggest that the genes responsible for wing and body colour in B. mori may be associated with similar genes in other Lepidoptera.

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Mutations of an Arylalkylamine-N-acetyltransferase, Bm-iAANAT, Are Responsible for Silkworm Melanism Mutant

Cited by 89 publications

References 35 publications

Mutation of a Cuticular Protein,BmorCPR2, Alters Larval Body Shape and Adaptability in Silkworm,Bombyx mori

Mutation of a Cuticular Protein,BmorCPR2, Alters Larval Body Shape and Adaptability in Silkworm,Bombyx mori

Drastic neofunctionalization associated with evolution of the timezyme AANAT 500 Mya

Mapping and recombination analysis of two moth colour mutations, Black moth and Wild wing spot, in the silkworm Bombyx mori

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