BmVMP90, a large vitelline membrane protein of the domesticated silkmoth Bombyx mori, is an essential component of the developing ovarian follicle

2012 ◽  
Vol 42 (9) ◽  
pp. 717-727 ◽  
Author(s):  
Nadia Sdralia ◽  
Luc Swevers ◽  
Kostas Iatrou
Keyword(s):  
Membrane Protein ◽  
Bombyx Mori ◽  
Ovarian Follicle ◽  
Vitelline Membrane ◽  
Essential Component

Expression of a vitelline membrane protein, BmVMP 23, is repressed by bmo-miR-1a-3p in silkworm, Bombyx mori

FEBS Letters ◽  
2013 ◽  
Vol 587 (7) ◽  
pp. 970-975 ◽  
Author(s):  
Anli Chen ◽  
Dingguo Xia ◽  
Zhiyong Qiu ◽  
Peng Gao ◽  
Shunming Tang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Bombyx Mori ◽  
Vitelline Membrane ◽  
Silkworm Bombyx Mori

Mutation of a vitelline membrane protein, BmEP80, is responsible for the silkworm “Ming” lethal egg mutant

Gene ◽  
2013 ◽  
Vol 515 (2) ◽  
pp. 313-319 ◽  
Author(s):  
Anli Chen ◽  
Peng Gao ◽  
Qiaoling Zhao ◽  
Shunming Tang ◽  
Xingjia Shen ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Vitelline Membrane

Studies on the Ovarian Follicle Cells of Drosophila

1963 ◽  
Vol s3-104 (67) ◽  
pp. 297-320
Author(s):  
R. C. KING ◽  
ELIZABETH A. KOCH
Keyword(s):  
Ovarian Follicle ◽  
Protein A ◽  
Follicle Cell ◽  
Follicle Cells ◽  
Vitelline Membrane ◽  
Membrane Material ◽  
Adjacent Layer ◽  
Membrane Formation ◽  
Precursor Material ◽  
Egg Shell

Studies are described of the ultrastructure of the follicle cells which invest the oocyte of Drosophila melanogaster at the time of vitelline membrane formation. Of particular interest are organelles made up of endoplasmic reticulum organized into a husk of concentric lamellae which surround lipidal droplets. These epithelial bodies are seen only at the time the vitelline membrane is being formed, and it is assumed therefore that the lipidal material of the epithelial body may be utilized somehow in the fabrication of the vitelline membrane. Cytochemical studies have shown this membrane to contain at least 5 classes of compounds; a protein, two lipids (which may be distinguished by differences in their resistance to extraction by various solvents), and 2 polysaccharides (1 neutral and 1 acidic). Studies were made of vitelline membrane formation in the ovaries of flies homozygous for either of 2 recessive, female-sterile genes (tiny and female sterile). In the case of the ty mutation vitelline membrane material is sometimes secreted between follicle and nurse cells, while in the mutant fes vitelline membrane is observed in rare instances to be secreted between follicle cells and an adjacent layer of tumour cells. In the latter case the vitelline membrane shows altered cytochemical properties. The fact that vitelline membrane can be secreted by follicle cells not adjacent to an oocyte demonstrates that it is the follicle cell rather than the oocyte that plays the major role in the secretion of the precursor material of the vitelline membrane. Subsequently the follicle cells secrete the egg-shell, or chorion, which is subdivided into a dense, compartmented, inner endochorion, and a pale, outer exochorion. A description is given of the ultrastructure of the follicle cells during the secretion of the endochorion and the exochorion. The endochorion contains a protein, a polysaccharide, and a lipid, all of which may be distinguished cytochemically from the vitelline membrane compounds. The exochorion contains large amounts of acidic mucopolysaccharides. Specialized follicle cells form the micropylar apparatus and the chorionic appendages. The formation of the chorion and chorionic appendages is discussed in the light of information gained from abnormalities of the chorions and chorionic appendages seen in ty and fs 2.1 oocytes. Subsequent to the time the egg leaves the ovariole a layer of waterproofing wax is secreted between the vitelline membrane and the chorion.

scholarly journals Localization of a novel 252-kDa plasma membrane protein that binds Cry1A toxins in the midgut epithelia of Bombyx mori

2005 ◽  
Vol 40 (1) ◽  
pp. 125-135 ◽  
Author(s):  
Delwer M. Hossain ◽  
Yasuyuki Shitomi ◽  
Yohei Nanjo ◽  
Daisuke Takano ◽  
Tadayuki Nishiumi ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Bombyx Mori ◽  
Plasma Membrane Protein

scholarly journals Formation of a β-barrel membrane protein is catalyzed by the interior surface of the assembly machine protein BamA

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
James Lee ◽  
David Tomasek ◽  
Thiago MA Santos ◽  
Mary D May ◽  
Ina Meuskens ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Molecular Mechanisms ◽  
Gram Negative Bacteria ◽  
Site Specific ◽  
Gram Negative ◽  
Interior Surface ◽  
Essential Component ◽  
Bam Complex ◽  
Β Sheet

The β-barrel assembly machine (Bam) complex in Gram-negative bacteria and its counterparts in mitochondria and chloroplasts fold and insert outer membrane β-barrel proteins. BamA, an essential component of the complex, is itself a β-barrel and is proposed to play a central role in assembling other barrel substrates. Here, we map the path of substrate insertion by the Bam complex using site-specific crosslinking to understand the molecular mechanisms that control β-barrel folding and release. We find that the C-terminal strand of the substrate is stably held by BamA and that the N-terminal strands of the substrate are assembled inside the BamA β-barrel. Importantly, we identify contacts between the assembling β-sheet and the BamA interior surface that determine the rate of substrate folding. Our results support a model in which the interior wall of BamA acts as a chaperone to catalyze β-barrel assembly.

Identification of a hemocyte membrane protein of the silkworm, Bombyx mori, which specifically binds to bacterial lipopolysaccharide

1995 ◽  
Vol 25 (8) ◽  
pp. 921-928 ◽  
Author(s):  
Jinhua Xu ◽  
Masahiro Nishijima ◽  
Yoshiaki Kono ◽  
Kiyoko Taniai ◽  
Yusuke Kato ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Bombyx Mori ◽  
Bacterial Lipopolysaccharide ◽  
Silkworm Bombyx Mori

Molecular characterization of a peritrophic membrane protein from the silkworm, Bombyx mori

2012 ◽  
Vol 40 (2) ◽  
pp. 1087-1095 ◽  
Author(s):  
Xiaolong Hu ◽  
Lin Chen ◽  
Rui Yang ◽  
Xingwei Xiang ◽  
Xiaofeng Wu
Keyword(s):  
Membrane Protein ◽  
Bombyx Mori ◽  
Molecular Characterization ◽  
Peritrophic Membrane ◽  
Silkworm Bombyx Mori
Sign in / Sign up

Export Citation Format

Share Document