scholarly journals Identification and Functional Analysis of BmNPV-Interacting Proteins From Bombyx mori (Lepidoptera) Larval Midgut Based on Subcellular Protein Levels

2020 ◽  
Vol 11 ◽  
Author(s):  
Shang-zhi Zhang ◽  
Lin-bao Zhu ◽  
Dong Yu ◽  
Ling-ling You ◽  
Jie Wang ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Bombyx Mori ◽  
Interacting Proteins ◽  
Larval Midgut ◽  
Protein Levels

Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori

2007 ◽  
Vol 1769 (9-10) ◽  
pp. 559-568 ◽  
Author(s):  
Hiromitsu Tanaka ◽  
Hiroyuki Matsuki ◽  
Seiichi Furukawa ◽  
Aki Sagisaka ◽  
Eiji Kotani ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Bombyx Mori ◽  
Silkworm Bombyx Mori

scholarly journals Proteomic analysis of Drosophila CLOCK complexes identifies rhythmic interactions with SAGA and Tip60 complex component NIPPED-A

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Guruswamy Mahesh ◽  
Gustavo B. S. Rivas ◽  
Courtney Caster ◽  
Evan B. Ost ◽  
Ravi Amunugama ◽  
...  
Keyword(s):  
Feedback Loop ◽  
Clock Cycle ◽  
Protein A ◽  
Interacting Proteins ◽  
Saga Complex ◽  
Protein Levels ◽  
Genes Encoding ◽  
Circadian Behavior ◽  
Transcriptional Output ◽  
Transcriptional Feedback

Abstract Circadian clocks keep time via ~ 24 h transcriptional feedback loops. In Drosophila, CLOCK-CYCLE (CLK-CYC) activators and PERIOD-TIMELESS (PER-TIM) repressors are feedback loop components whose transcriptional status varies over a circadian cycle. Although changes in the state of activators and repressors has been characterized, how their status is translated to transcriptional activity is not understood. We used mass spectrometry to identify proteins that interact with GFP-tagged CLK (GFP-CLK) in fly heads at different times of day. Many expected and novel interacting proteins were detected, of which several interacted rhythmically and were potential regulators of protein levels, activity or transcriptional output. Genes encoding these proteins were tested to determine if they altered circadian behavior via RNAi knockdown in clock cells. The NIPPED-A protein, a scaffold for the SAGA and Tip60 histone modifying complexes, interacts with GFP-CLK as transcription is activated, and reducing Nipped-A expression lengthens circadian period. RNAi analysis of other SAGA complex components shows that the SAGA histone deubiquitination (DUB) module lengthened period similarly to Nipped-A RNAi knockdown and weakened rhythmicity, whereas reducing Tip60 HAT expression drastically weakened rhythmicity. These results suggest that CLK-CYC binds NIPPED-A early in the day to promote transcription through SAGA DUB and Tip60 HAT activity.

scholarly journals Clone and functional analysis of Seryl-tRNA synthetase and Tyrosyl-tRNA synthetase from silkworm, Bombyx mori

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Jingsheng Hu ◽  
Jianghai Tian ◽  
Fanchi Li ◽  
Bin Xue ◽  
Jiahuan Hu ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Bombyx Mori ◽  
Trna Synthetase ◽  
Silkworm Bombyx Mori

Purification of glycosylphosphatidylinositol-anchoring aminopeptidase in from the plasma membrane of larval midgut epithelial cells of the silkworm, Bombyx mori

1994 ◽  
Vol 26 (8) ◽  
pp. 977-986 ◽  
Author(s):  
Tomita Masahiro ◽  
Obara Hiroshi ◽  
Takesue Yoshiki ◽  
Tamura Hiro-Omi ◽  
Miyajima Shigetoshi ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Bombyx Mori ◽  
Larval Midgut ◽  
Silkworm Bombyx Mori

Identification and functional analysis of the cathepsin D gene promoter of Bombyx mori

2014 ◽  
Vol 41 (3) ◽  
pp. 1623-1630 ◽  
Author(s):  
Jie Yu ◽  
Feng-Yao Wu ◽  
Feng-Ming Zou ◽  
Xiang-Yun Cai ◽  
Hai-Yan Yu ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Bombyx Mori ◽  
Cathepsin D ◽  
Gene Promoter

scholarly journals Functional analysis of Bombyx mori Decapentaplegic gene for bone differentiation in a mammalian cell

2013 ◽  
Vol 27 (1) ◽  
pp. 159-165 ◽  
Author(s):  
Seung-Won Park ◽  
Tae-Won Goo ◽  
Gwang-Ho Choi ◽  
Seok-Woo Kang ◽  
Sung-Wan Kim ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Bombyx Mori ◽  
Mammalian Cell ◽  
Bone Differentiation

scholarly journals Tip60 Phosphorylation at Ser 99 Is Essential for Autophagy Induction in Bombyx mori

2020 ◽  
Vol 21 (18) ◽  
pp. 6893
Author(s):  
Wenmei Wu ◽  
Kang Li ◽  
Haigang Zhao ◽  
Xianying Xu ◽  
Jing Xu ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Histone Acetyltransferase ◽  
Regulatory Mechanism ◽  
Fat Body ◽  
Critical Role ◽  
Phosphorylation Site ◽  
Protein Levels ◽  
Autophagy Induction ◽  
Phosphatase Treatment ◽  
Amp Activated Protein Kinase

Tip60, a key histone acetyltransferase of the MYST family and member of the nuclear multimeric protein complex (NuA4), regulates the activity and stability of proteins involved in the cell cycle, DNA damage responses, autophagy, etc. However, the function and regulatory mechanism of Tip60 homolog in Bombyx mori are not elucidated. In the present study, Bombyx Tip60 (BmTip60) was functionally identified. Developmental profiles showed that the protein levels and nuclear localization of BmTip60 peaked in fat body during the larval–pupal metamorphosis when autophagy was intensive; simultaneously, the BmTip60 protein migrated to form an upper band as detected by Western blot. Interestingly, the upper band of BmTip60 was reduced by λ-phosphatase treatment, indicating that it was a phosphorylated form of BmTip60. Results showed that BmTip60 was promoted by starvation but not 20-hydroxyecdysone treatment. Transcription factor AMP-activated protein kinase (AMPK) affected by starvation was pivotal for BmTip60 protein migration. In addition, one mammalian phosphorylation site was identified in BmTip60 at Ser99, the constitutive-activation mutation of Ser99 to Asp99 but not its inactive mutation to Ala99 significantly upregulated autophagy, showing the critical role of phosphorylation at Ser99 for BmTip60-mediated autophagy. In conclusion, the starvation-AMPK axis promotes BmTip60 in B. mori, which was requisite for autophagy induction. These results reveal a regulatory mechanism of histone acetyltransferase Tip60 homologs by phosphorylation in insects, and sheds light on further related studies of acetylation regulation.

The midgut of the silkmoth Bombyx mori is able to recycle molecules derived from degeneration of the larval midgut epithelium

2015 ◽  
Vol 361 (2) ◽  
pp. 509-528 ◽  
Author(s):  
Eleonora Franzetti ◽  
Davide Romanelli ◽  
Silvia Caccia ◽  
Silvia Cappellozza ◽  
Terenzio Congiu ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Midgut Epithelium ◽  
Larval Midgut
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