scholarly journals Genome-Wide Identification and Characterization of Amino Acid Polyamine Organocation Transporter Family Genes Reveal Their Role in Fecundity Regulation in a Brown Planthopper Species (Nilaparvata lugens)

2021 ◽  
Vol 12 ◽  
Author(s):  
Lei Yue ◽  
Ziying Guan ◽  
Mingzhao Zhong ◽  
Luyao Zhao ◽  
Rui Pang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gene Family ◽  
Quantitative Polymerase Chain Reaction ◽  
Expression Patterns ◽  
Regulatory Gene ◽  
Brown Planthopper ◽  
Nilaparvata Lugens ◽  
Functional Domain ◽  
Common Amino Acid

The brown planthopper (BPH), Nilaparvata lugens Stål (Hemiptera:Delphacidae), is one of the most destructive pests of rice worldwide. As a sap-feeding insect, the BPH is incapable of synthesizing several amino acids which are essential for normal growth and development. Therefore, the insects have to acquire these amino acids from dietary sources or their endosymbionts, in which amino acid transporters (AATs) play a crucial role by enabling the movement of amino acids into and out of insect cells. In this study, a common amino acid transporter gene family of amino acid/polyamine/organocation (APC) was identified in BPHs and analyzed. Based on a homology search and conserved functional domain recognition, 20 putative APC transporters were identified in the BPH genome. Molecular trait analysis showed that the verified BPH APC family members were highly variable in protein features, conserved motif distribution patterns, and exon/intron organization. Phylogenetic analysis of five hemipteran species revealed an evolutionary pattern of interfamily conservation and lineage-specific expansion of this gene family. Moreover, stage- and tissue-specific expression analysis revealed diverse expression patterns in the 20 BPH APC transporter genes. Lastly, a potential BPH fecundity regulatory gene of NlAPC09 was identified and shown to participate in the fecundity regulation through the use of quantitative polymerase chain reaction (qPCR) and RNA inference experiments. Our results provide a basis for further functional investigations of APC transporters in BPH.

scholarly journals Genome-Wide Analysis of the Amino Acid Auxin Permease (AAAP) Gene Family and Identification of an AAAP Gene Associated with the Growth and Reproduction of the Brown Planthopper, Nilaparvata lugens (Stål)

Insects ◽  
2021 ◽  
Vol 12 (8) ◽  
pp. 746
Author(s):  
Lei Yue ◽  
Rui Pang ◽  
Hu Tian ◽  
Ziying Guan ◽  
Mingzhao Zhong ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gene Family ◽  
Brown Planthopper ◽  
Larval Growth ◽  
Family Members ◽  
Nilaparvata Lugens ◽  
Hatching Rate ◽  
Characteristic Analysis ◽  
Transporter Family

Amino acids play a vital role in several biological processes in organisms and are mainly acquired through diet by most insects. The amino acid auxin permease (AAAP) transporter family is an important amino acid transporter gene family in insects for the transportation of amino acids into and out of cells across the plasma membrane. Here, we identified 21 putative AAAP family members in the genome of the brown planthopper (BPH), Nilaparvata lugens, a devastating pest that feeds only on the phloem sap of rice plants. Molecular characteristic analysis indicated large variations in protein features and amino acid sequences among the predicted AAAP family members in BPH. Phylogenetic analysis clustered these AAAP transporters into three subgroups, with the members in the same group sharing a similar pattern of conserved motif distribution. Through ortholog gene recognition and spatiotemporal gene expression analysis, the AAAP gene NlAAAP07, which was predicted to regulate BPH larval growth and female fecundity, was identified. RNA interference (RNAi)-mediated suppression of NlAAAP07 significantly postponed the duration of 3rd instar nymphs developing into adults from 7.4 days to 9.0 days, and decreased the oviposition amount and egg hatching rate of females by 30.7% and 11.0%, respectively. Our results provide a foundation for further functional analysis of AAAP transporters in BPH.

scholarly journals daf-7-related TGF-β homologues from Trichostrongyloid nematodes show contrasting life-cycle expression patterns

Parasitology ◽  
2009 ◽  
Vol 137 (1) ◽  
pp. 159-171 ◽  
Author(s):  
H. J. McSORLEY ◽  
J. R. GRAINGER ◽  
Y. HARCUS ◽  
J. MURRAY ◽  
A. J. NISBET ◽  
...  
Keyword(s):  
Amino Acids ◽  
Life Cycle ◽  
Gene Family ◽  
Transforming Growth Factor ◽  
Signal Sequence ◽  
Expression Patterns ◽  
Transforming Growth Factor Β ◽  
Laboratory Model ◽  
Parasitic Nematodes ◽  
Nippostrongylus Brasiliensis

SUMMARYThe transforming growth factor-β (TGF-β) gene family regulates critical processes in animal development, and plays a crucial role in regulating the mammalian immune response. We aimed to identify TGF-β homologues from 2 laboratory model nematodes (Heligmosomoides polygyrus and Nippostrongylus brasiliensis) and 2 major parasites of ruminant livestock (Haemonchus contortus and Teladorsagia circumcincta). Parasite cDNA was used as a template for gene-specific PCR and RACE. Homologues of the TGH-2 subfamily were isolated, and found to differ in length (301, 152, 349 and 305 amino acids respectively), with variably truncated N-terminal pre-proteins. All contained conserved C-terminal active domains (>85% identical over 115 amino acids) containing 9 cysteine residues, as in C. elegans DAF-7, Brugia malayi TGH-2 and mammalian TGF-β. Surprisingly, only the H. contortus homologue retained a conventional signal sequence, absent from shorter proteins of other species. RT-PCR assays of transcription showed that in H. contortus and N. brasiliensis expression was maximal in the infective larval stage, and very low in adult worms. In contrast, in H. polygyrus and T. circumcincta, tgh-2 transcription is higher in adults than infective larvae. The molecular evolution of this gene family in parasitic nematodes has diversified the pre-protein and life-cycle expression patterns of TGF-β homologues while conserving the structure of the active domain.

scholarly journals The Amino Acid Permeases AAP3 and AAP6 Are Involved in Root-Knot Nematode Parasitism of Arabidopsis

2013 ◽  
Vol 26 (1) ◽  
pp. 44-54 ◽  
Author(s):  
Heather H. Marella ◽  
Erik Nielsen ◽  
Daniel P. Schachtman ◽  
Christopher G. Taylor
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Expression Patterns ◽  
Giant Cells ◽  
Root Knot Nematode ◽  
Egg Hatching ◽  
Feeding Site ◽  
Vascular Tissues ◽  
Nematode Parasitism ◽  
Amino Acid Permeases

The root-knot nematode, Meloidogyne incognita, is an obligate parasite which depends entirely on the host plant for its nutrition. Root-knot nematodes induce the formation of a highly specialized feeding site consisting of several giant cells surrounded by a network of vascular tissues. Nutrients, including amino acids and sugars, are transferred apoplastically from the vascular tissues to the feeding site. Using Arabidopsis thaliana lacking the vascular-expressed amino acid permeases (AAP) AAP3 or AAP6, we demonstrate that disruption of amino acid transport can affect nematode parasitism. Nematode infestation levels are significantly reduced on the aap3 and aap6 mutants. AAP3 and AAP6 act distinctly in the transport of amino acids to the feeding site, as demonstrated by differences in their carrying capacity profiles. Furthermore, analyses of promoter: β-glucuronidase lines show different expression patterns for AAP3 and AAP6 in infected roots. In the aap3-3 mutant, part of the decrease in infestation is connected to a defect in early infection, where juveniles enter but then leave the root. Both aap3-3 and aap6-1 produce fewer females and produce more adult male nematodes. Additionally, detrimental effects are observed in the nematodes harvested from aap3-3 and aap6-1 mutants, including decreased egg hatching and infectivity and lower levels of lipid reserves. The transport of amino acids by AAP3 and AAP6 is important for nematode infection and success of the progeny.

scholarly journals Organizational analysis of elav gene and functional analysis of ELAV protein of Drosophila melanogaster and Drosophila virilis.

1991 ◽  
Vol 11 (6) ◽  
pp. 2994-3000 ◽  
Author(s):  
K M Yao ◽  
K White
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Rna Binding ◽  
Terminal Region ◽  
Drosophila Virilis ◽  
Functional Domain ◽  
Amino Terminal ◽  
Binding Domains ◽  
Rna Binding Domains

Drosophila virilis genomic DNA corresponding to the D. melanogaster embryonic lethal abnormal visual system (elav) locus was cloned. DNA sequence analysis of a 3.8-kb genomic piece allowed identification of (i) an open reading frame (ORF) with striking homology to the previously identified D. melanogaster ORF and (ii) conserved sequence elements of possible regulatory relevance within and flanking the second intron. Conceptual translation of the D. virilis ORF predicts a 519-amino-acid-long ribonucleoprotein consensus sequence-type protein. Similar to D. melanogaster ELAV protein, it contains three tandem RNA-binding domains and an alanine/glutamine-rich amino-terminal region. The sequence throughout the RNA-binding domains, comprising the carboxy-terminal 346 amino acids, shows an extraordinary 100% identity at the amino acid level, indicating a strong structural constraint for this functional domain. The amino-terminal region is 36 amino acids longer in D. virilis, and the conservation is 66%. In in vivo functional tests, the D. virilis ORF was indistinguishable from the D. melanogaster ORF. Furthermore, a D. melanogaster ORF encoding an ELAV protein with a 40-amino-acid deletion within the alanine/glutamine-rich region was also able to supply elav function in vivo. Thus, the divergence of the amino-terminal region of the ELAV protein reflects lowered functional constraint rather than species-specific functional specification.

Molecular characterization, expression analysis and RNAi knock-down of elongation factor 1α and 1γ from Nilaparvata lugens and its yeast-like symbiont

2016 ◽  
Vol 107 (3) ◽  
pp. 303-312 ◽  
Author(s):  
W.X. Wang ◽  
T.H. Zhu ◽  
K.L. Li ◽  
L.F. Chen ◽  
F.X. Lai ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Homology ◽  
Fat Body ◽  
Quantitative Polymerase Chain Reaction ◽  
Elongation Factor ◽  
Nilaparvata Lugens ◽  
Expression Level ◽  
Amino Acid Sequence Homology ◽  
Qpcr Analysis

AbstractIn the present paper, four cDNAs encoding the alpha and gamma subunits of elongation factor 1 (EF-1) were cloned and sequenced from Nilaparvata lugens, named NlEF-1α, NlEF-1γ, and its yeast-like symbiont (YLS), named YsEF-1α and YsEF-1γ, respectively. Comparisons with sequences from other species indicated a greater conservation for EF-1α than for EF-1γ. NlEF-1α has two identical copies. The deduced amino acid sequence homology of NlEF-1α and NlEF-1γ is 96 and 64%, respectively, compared with Homalodisca vitripennis and Locusta migratoria. The deduced amino acid sequence homology of YsEF-1α and YsEF-1γ is 96 and 74%, respectively, compared with Metarhizium anisopliae and Ophiocordyceps sinensis. Reverse transcription-quantitative polymerase chain reaction (RT–qPCR) analysis revealed that the expression level of NlEF-1α and NlEF-1γ mRNA in hemolymph, ovary, fat body and salivary glands were higher than the midgut and leg tissue. YsEF-1α and YsEF-1γ was highly expressed in fat body. The expression level of NlEF-1α was higher than that of NlEF-1γ. Through RNA interference (RNAi) of the two genes, the mortality of nymph reached 92.2% at the 11th day after treatment and the ovarian development was severely hindered. The RT–qPCR analysis verified the correlation between mortality, sterility and the down-regulation of the target genes. The expression and synthesis of vitellogenin (Vg) protein in insects injected with NlEF-1α and NlEF-1γ double-stranded RNA (dsRNA) was significantly lower than control groups. Attempts to knockdown the YsEF-1 genes in the YLS was unsuccessful. However, the phenotype of N. lugens injected with YsEF-1α dsRNA was the same as that injected with NlEF-1α dsRNA, possibly due to the high similarity (up to 71.9%) in the nucleotide sequences between NlEF-1α and YsEF-1α. We demonstrated that partial silencing of NlEF-1α and NlEF-1γ genes caused lethal and sterility effect on N. lugens. NlEF-1γ shares low identity with that of other insects and therefore it could be a potential target for RNAi-based pest management.

scholarly journals A Mating-Induced Protein of Phytophthora infestans Is a Member of a Family of Elicitors with Divergent Structures and Stage-Specific Patterns of Expression

2003 ◽  
Vol 16 (10) ◽  
pp. 926-935 ◽  
Author(s):  
Anna-Liisa Fabritius ◽  
Howard S. Judelson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gene Family ◽  
Phytophthora Infestans ◽  
Amino Acid Identity ◽  
Acid Identity ◽  
Terminal Domain ◽  
Defense Reactions ◽  
The Family ◽  
Microbe Interactions

Five members of an elicitor-like gene family from Phytophthora infestans were examined. The family was identified through the analysis of M81, a mating-induced gene. The predicted M81 product resembled a 42-kDa P. sojae glycoprotein known to elicit defense reactions in plants, including a host of P. infestans, potato. M81 was the most structurally and functionally divergent of the P. infestans genes compared with the P. sojae sequence. M81 lacked elicitor activity, had the lowest protein identity (47%), displayed mating-specific transcription, and had a novel C-terminal domain. The latter contained a 30-residue proline- and threonine-rich motif, which, remarkably, was tandemly repeated 24 to 36 times in different alleles. M81C, M81D, and M81E better resembled the P. sojae protein based on amino acid identity (63 to 75%) and conserved elicitor activity. M81C and M81D mRNA accumulated only during zoosporogenesis, while M81E expression was restricted to hyphae. M81B, an apparent pseudogene, was physically linked to M81. The protein products of each gene were predicted to be extracellular transglutaminases ranging in size from 436 to 1,607 amino acids. Genes with an elicitor, proline- and threonine-rich repeat, and both elicitor and repeat domains were widely distributed throughout Phytophthora infestans. These findings help explain the natural functions of elicitors in pathogen biology and plant-microbe interactions.

scholarly journals Identification and expression analysis of the WRKY gene family during different developmental stages in Lycium ruthenicum Murr. fruit

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e10207
Author(s):  
Richard John Tiika ◽  
Jia Wei ◽  
Rui Ma ◽  
Hongshan Yang ◽  
Guangxin Cui ◽  
...  
Keyword(s):  
Gene Family ◽  
Plant Species ◽  
Zinc Finger ◽  
Developmental Stages ◽  
Quantitative Polymerase Chain Reaction ◽  
Expression Patterns ◽  
Conserved Motif ◽  
Motif Prediction ◽  
Transcriptome Database ◽  
Lycium Ruthenicum

Background The WRKY gene family, one of the major transcription factor families in plants, plays crucial regulatory roles in physiological and biological developmental processes, and the adaptation of plants to the environment. However, the systematic study of WRKY structure, expression profiling, and regulatory functions has not been extensively reported in Lycium ruthenicum, although these aspects have been comprehensively studied in most plant species. Methods In this study, the WRKY genes were identified from a L. ruthenicum transcriptome database by using bioinformatics. The identification, phylogenetic analysis, zinc-finger structures, and conserved motif prediction were extensively explored. Moreover, the expression levels of 23 selected genes with fragments per kilobase of exons per million mapped reads (FPKM) >5 were assayed during different fruit developmental stages with real-time quantitative polymerase chain reaction (RT-qPCR). Results A total of 73 putative WRKY proteins in the L. ruthenicum transcriptome database were identified and examined. Forty-four proteins with the WRKY domain were identified and divided into three major groups with several subgroups, in accordance with those in other plant species. All 44 LrWRKY proteins contained one or two conserved WRKY domains and a zinc-finger structure. Conserved motif prediction revealed conservation of the WRKY DNA-binding domain in L. ruthenicum proteins. The selected LrWRKY genes exhibited discrete expression patterns during different fruit developmental stages. Interestingly, five LrWRKYs (-20, -21, -28, -30, and -31) were expressed remarkably throughout the fruit developmental stages. Discussion Our results reveal the characteristics of the LrWRKY gene family, thus laying a foundation for further functional analysis of the WRKY family in L. ruthenicum.

Identification and Characterisation of Two 1-Aminocyclopropane- 1-Carboxylate (ACC) Synthase cDNAs Expressed during Papaya (Carica papaya) Fruit Ripening

1997 ◽  
Vol 24 (2) ◽  
pp. 239 ◽  
Author(s):  
Michael Glenn Mason ◽  
José Ramón Botella
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Fruit Ripening ◽  
Active Site ◽  
Carica Papaya ◽  
Expression Patterns ◽  
Acc Synthase ◽  
Single Copy ◽  
Mrna Levels ◽  
Amino Acid Residues

The cloning and characterisation of two cDNAs (capacs1 and capacs2) encoding ACC synthase in papaya (Carica papaya L.) is described. capacs1 is 1104 bp long encoding 368 amino acids. capacs2 is 1098 bp long encoding 366 amino acids. The proteins encoded by both cDNAs contain the highly conserved active site of ACC synthases as well as 10 (capacs1) or 11 (capacs2) of the 12 amino acid residues conserved in most aminotransferases. Southern analyses indicate that capacs1 and capacs2 are present in the papaya genome as single copy genes. Both genes show very different expression patterns during fruit ripening. capacs1 mRNA levels are high in mature green fruits, decreasing steadily during ripening, whereas capacs2 mRNA levels are undetectable in mature green fruits but experience a dramatic increase with the onset of ripening and remain high throughout the various stages of ripening.

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