کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8357858 | 1542056 | 2015 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Protein-protein interactions among enzymes of starch biosynthesis in high-amylose barley genotypes reveal differential roles of heteromeric enzyme complexes in the synthesis of A and B granules
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کلمات کلیدی
su2DBESDSAMGHAGamylose extenderPho1APaseGPCGBSSAGPaseSBEAdenosine Triphosphate - آدنوزین تری فسفاتATP - آدنوزین تری فسفات یا ATPAlkaline phosphatase - آلکالین فسفاتاز یا فسفاتاز قلیاییAmyloglucosidase - آمیلوگلوکوزیدازstarch debranching enzyme - آنزیم انحلال نشاستهstarch branching enzyme - آنزیم شاخه ای نشاسته ای استStarch biosynthesis - بیوسنتز نشاستهBarley - جو dalton - دالتونsodium dodecyl sulphate - سدیم دودسیل سولفاتEnzyme complexes - مجتمع های آنزیمstarch synthase - نشاسته سنتازStarch phosphorylase - نشاسته فسفریلاسISA - هست یکPullulanase - پولولنازGel permeation chromatography - کروماتوگرافی ژل تراوشیgranule bound starch synthase - گرانول نشاسته سنتاز متصل شده است
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The present study investigated the role of protein phosphorylation, and protein complex formation between key enzymes of amylopectin synthesis, in barley genotypes exhibiting “high amylose” phenotypes. Starch branching enzyme (SBE) down-regulated lines (ÎSBEIIa and ÎSBEIIb), starch synthase (SS)IIa (ssiiaâ, sex6) and SSIII (ssiiiâ, amo1) mutants were compared to a reference genotype, OAC Baxter. Down-regulation of either SBEIIa or IIb caused pleiotropic effects on SSI and starch phosphorylase (SP) and resulted in formation of novel protein complexes in which the missing SBEII isoform was substituted by SBEI and SP. In the ÎSBEIIb down-regulated line, soluble SP activity was undetectable. Nonetheless, SP was incorporated into a heteromeric protein complex with SBEI and SBEIIa and was readily detected in starch granules. In amo1, unlike other mutants, the data suggest that both SBEIIa and SBEIIb are in a protein complex with SSI and SSIIa. In the sex6 mutant no protein complexes involving SBEIIa or SBEIIb were detected in amyloplasts. Studies with Pro-Q Diamond revealed that GBSS, SSI, SSIIa, SBEIIb and SP are phosphorylated in their granule bound state. Alteration in the granule proteome in ÎSBEIIa and ÎSBEIIb lines, suggests that different protein complexes are involved in the synthesis of A and B granules.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Science - Volume 233, April 2015, Pages 95-106
Journal: Plant Science - Volume 233, April 2015, Pages 95-106
نویسندگان
Zaheer Ahmed, Ian J. Tetlow, Regina Ahmed, Matthew K. Morell, Michael J. Emes,