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Two calcium‐binding chaperones from the fat body of the Colorado potato beetle, Leptinotarsa decemlineata (Coleoptera: Chrysomelidae) involved in diapause
Archives of Insect Biochemistry and Physiology ( IF 2.2 ) Pub Date : 2020-10-28 , DOI: 10.1002/arch.21755
Cansu Doğan 1, 2, 3, 4 , Sabine Hänniger 2 , David G. Heckel 2 , Cathy Coutu 3 , Dwayne D. Hegedus 3 , Linda Crubaugh 4 , Russell L. Groves 4 , Şerife Bayram 1 , Umut Toprak 1
Affiliation  

Molecular chaperones are crucial for the correct folding of newly synthesized polypeptides, in particular, under stress conditions. Various studies have revealed the involvement of molecular chaperones, such as heat shock proteins, in diapause maintenance and starvation; however, the role of other chaperones in diapause and starvation relatively is unknown. In the current study, we identified two lectin‐type chaperones with calcium affinity, a calreticulin (LdCrT) and a calnexin (LdCnX), that were present in the fat body of the Colorado potato beetle, Leptinotarsa decemlineata (Coleoptera: Chrysomelidae) during diapause. Both proteins possessed an N‐globular domain, a P‐arm domain, and a highly charged C‐terminal domain, while an additional transmembrane domain was present in LdCnX. Phylogenetic analysis revealed distinction at the order level. Both genes were expressed in multiple tissues in larval and adult stages, and constitutively throughout development, though a starvation response was detected only for LdCrT. In females, diapause‐related expression analysis in the whole body revealed an upregulation of both genes by post‐diapause, but a downregulation by diapause only for LdCrT. By contrast, males revealed no alteration in their diapause‐related expression pattern in the entire body for both genes. Fat body‐specific expression analysis of both genes in relation to diapause revealed the same expression pattern with no alteration in females and downregulation in males by post‐diapause. This study suggests that calcium‐binding chaperones play similar and possibly gender‐specific roles during diapause.

中文翻译:

来自科罗拉多马铃薯甲虫脂肪的两个钙结合伴侣蛋白,Leptinotarsa decemlineata(鞘翅目:金眼科)参与滞育

分子伴侣对于新合成多肽的正确折叠至关重要,特别是在压力条件下。各种研究表明,分子伴侣蛋白(例如热休克蛋白)参与滞育维持和饥饿。然而,其他伴侣在滞育和饥饿中的作用相对未知。在本研究中,我们鉴定出科罗拉多马铃薯甲虫Leptinotarsa decemlineata的脂肪体内存在两种具有钙亲和力的凝集素型分子伴侣,即钙网蛋白(LdCrT)和钙质蛋白(LdCnX)。滞育期间(鞘翅目:金眼科)。两种蛋白质都具有一个N球状结构域,一个P臂结构域和一个带高电荷的C末端结构域,而LdCnX中存在一个额外的跨膜结构域。系统发育分析揭示了在顺序级别上的区别。两种基因均在幼虫和成虫的多个组织中表达,并在整个发育过程中组成性表达,尽管仅对LdCrT检测到饥饿反应。在女性中,整个滞育相关的表达分析表明,滞育后两种基因均上调,而滞育仅对LdCrT上调。。相比之下,雄性显示这两种基因在整个滞育期的表达方式都没有改变。两种基因与滞育相关的脂肪体特异性表达分析显示,相同的表达模式在女性中没有改变,而在男性角色中却没有因滞后引起的下调。这项研究表明,钙滞留的伴侣在滞育过程中起着类似的作用,并且可能具有性别特异性。
更新日期:2020-12-26
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