کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10767762 | 1050796 | 2005 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
BmStart1, a novel carotenoid-binding protein isoform from Bombyx mori, is orthologous to MLN64, a mammalian cholesterol transporter
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Carotenoid-binding protein (CBP) from the silkworm Bombyx mori is an essential molecule for carotenoid dependent cocoon pigmentation. We identified a novel isoform of CBP, Start1 of B. mori (BmStart1). BmStart1 contains a membrane-spanning MENTAL domain in its N-terminus and a lipid-binding START domain in its C-terminus. This domain architecture is identical to the mammalian MLN64 and Start1 of Drosophila melanogaster (DmStart1), both of which have been implicated to function in cholesterol transport and regulation of steroidogenesis. BmStart1 is expressed in both white and yellow cocoon strains of B. mori, while CBP is only detected in the yellow cocoon strain. BmStart1 mRNA abundance in the prothoracic gland, the main ecdysteroidogenic tissue, positively correlates with changes in the hemolymph ecdysteroid level. Genomic sequence analysis revealed that BmStart1 and CBP are generated from the same gene locus by alternative splicing. Splice site comparison and homology search indicate that BmStart1 is orthologous to both MLN64 and DmStart1. This study implies that alternative splicing of the BmStart1/CBP gene generates unique protein isoforms whose endogenous ligands, sterol or carotenoid, are structurally different.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 336, Issue 4, 4 November 2005, Pages 1125-1135
Journal: Biochemical and Biophysical Research Communications - Volume 336, Issue 4, 4 November 2005, Pages 1125-1135
نویسندگان
Takashi Sakudoh, Kozo Tsuchida, Hiroshi Kataoka,