کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2016671 | 1067678 | 2009 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Arabidopsis thaliana GPAT8 and GPAT9 are localized to the ER and possess distinct ER retrieval signals: Functional divergence of the dilysine ER retrieval motif in plant cells
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کلمات کلیدی
SNARELPATBY-2RFPGPATDGATConATMDSRPMCsACPConcanavalin AGFPDICORFArabidopsis thaliana - آرابیدوپسیس تالیاناFatty acid desaturase - اسید لاکتیک اسیدFAD - بدLocalization - بومی سازیtriacylglycerol - تری آسیل گلیسرول TAG یا triacylglycerols - تری گلیسرید یا تری آسیل گلیسرولtransmembrane domain - دامنه فرابنفشDiacylglycerol acyltransferase - دیسیللیسرول آکیلتانسفرازازBright Yellow-2 - روشن زرد-2multiple cloning site - سایت کلونینگ چندگانهendoplasmic reticulum - شبکه آندوپلاسمی open reading frame - قاب خواندن بازlysophosphatidic acid acyltransferase - لیسفسفید فسفیدید اسید آتیل ترانسفرازacyl-carrier protein - پروتئین حامل آسیلgreen fluorescent protein - پروتئین فلورسنت سبزred fluorescent protein - پروتئین فلورسنت قرمزLipids - چربیهاdifferential interference contrast - کنتراست تداخل دیفرانسیلglycerol-3-phosphate acyltransferase - گلیسرول 3-فسفات آتیل ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Glycerol-3-phosphate acyltransferase (GPAT; EC 2.3.1.15) catalyzes the committed step in the production of glycerolipids, which are major components of cellular membranes, seed storage oils, and epicuticular wax coatings. While the biochemical activities of GPATs have been characterized in detail, the cellular features of these enzymes are only beginning to emerge. Here we characterized the phylogenetic relationships and cellular properties of two GPAT enzymes from the relatively large Arabidopsis thaliana GPAT family, including GPAT8, which is involved in cutin biosynthesis, and GPAT9, which is a new putative GPAT that has extensive homology with a GPAT from mammalian cells involved in storage oil formation and, thus, may have a similar role in plants. Immunofluorescence microscopy of transiently-expressed myc-epitope-tagged GPAT8 and GPAT9 revealed that both proteins were localized to the endoplasmic reticulum (ER), and differential permeabilization experiments indicated that their N- and C-termini were oriented towards the cytosol. However, these two proteins contained distinct types of ER retrieval signals, with GPAT8 possessing a divergent type of dilysine motif (-KK-COOH rather than the prototypic -KKXX-COOH or -KXKXX-COOH motif) and GPAT9 possessing a hydrophobic pentapeptide motif (-Ï-X-X-K/R/D/E-Ï-; where Ï are large hydrophobic amino acid residues). Notably, the divergent dilysine motif in GPAT8 only functioned effectively when additional upstream residues were included to provide the proper protein context. Extensive mutational analyses of the divergent dilysine motif, based upon sequences present in the C-termini of other GPAT8s from various plant species, further expanded the functional definition of this molecular targeting signal, thereby providing insight to the targeting signals in other GPAT family members as well as other ER-resident membrane proteins within plant cells.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Physiology and Biochemistry - Volume 47, Issue 10, October 2009, Pages 867-879
Journal: Plant Physiology and Biochemistry - Volume 47, Issue 10, October 2009, Pages 867-879
نویسندگان
Satinder K. Gidda, Jay M. Shockey, Steven J. Rothstein, John M. Dyer, Robert T. Mullen,