title: Cloning and analysis of DnaJ family members in the silkworm, Bombyx mori.
abstract: Heat shock proteins (Hsps) are involved in a variety of critical biological functions, including protein folding, degradation, and translocation and macromolecule assembly, act as molecular chaperones during periods of stress by binding to other proteins. Using expressed sequence tag (EST) and silkworm (Bombyx mori) transcriptome databases, we identified 27 cDNA sequences encoding the conserved J domain, which is found in DnaJ-type Hsps. Of the 27 J domain-containing sequences, 25 were complete cDNA sequences. We divided them into three types according to the number and presence of conserved domains. By analyzing the gene structures, intron numbers, and conserved domains and constructing a phylogenetic tree, we found that the DnaJ family had undergone convergent evolution, obtaining new domains to expand the diversity of its family members. The acquisition of the new DnaJ domains most likely occurred prior to the evolutionary divergence of prokaryotes and eukaryotes. The expression of DnaJ genes in the silkworm was generally higher in the fat body. The tissue distribution of DnaJ1 proteins was detected by western blotting, demonstrating that in the fifth-instar larvae, the DnaJ1 proteins were expressed at their highest levels in hemocytes, followed by the fat body and head. We also found that the DnaJ1 transcripts were likely differentially translated in different tissues. Using immunofluorescence cytochemistry, we revealed that in the blood cells, DnaJ1 was mainly localized in the cytoplasm.
authors.affiliation: Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China. Electronic address: liyinv@caas.cn.
authors.forename: Yinü
authors.initials: Y
authors.lastname: Li
authors.affiliation: Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China. Electronic address: cuiyu2001@163.com.
authors.forename: Cuiyu
authors.initials: C
authors.lastname: Bu
authors.affiliation: Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China. Electronic address: ewuzh@163.com.
authors.forename: Tiantian
authors.initials: T
authors.lastname: Li
authors.affiliation: Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China. Electronic address: shizi0226@163.com.
authors.forename: Shibao
authors.initials: S
authors.lastname: Wang
authors.affiliation: Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China. Electronic address: jiangfeng330557624@163.com.
authors.forename: Feng
authors.initials: F
authors.lastname: Jiang
authors.affiliation: The Sericultural Research Institute, Chinese Academy of Agricultural Sciences, Zhenjiang, China. Electronic address: yiyongzhu@126.com.
authors.forename: Yongzhu
authors.initials: Y
authors.lastname: Yi
authors.affiliation: Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China. Electronic address: yhp97@hotmail.com.
authors.forename: Huipeng
authors.initials: H
authors.lastname: Yang
authors.affiliation: Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China. Electronic address: zhifangzhang@yahoo.com.
authors.forename: Zhifang
authors.initials: Z
authors.lastname: Zhang
mesh_terms: D000818:Animals; D012831:Bombyx / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D030541:Databases, Genetic; D005786:Gene Expression Regulation / Q000502:physiology*; D050956:HSP40 Heat-Shock Proteins / Q000096:biosynthesis / Q000235:genetics; D006434:Hemocytes / Q000378:metabolism; D019476:Insect Proteins / Q000096:biosynthesis / Q000235:genetics; D009928:Organ Specificity / Q000502:physiology; D010802:Phylogeny; D017434:Protein Structure, Tertiary
chemical_list: D050956:HSP40 Heat-Shock Proteins; D019476:Insect Proteins
keywords: Convergent evolution; DnaJ; Silkworm; Tissue expression profile