小麦 γ 醇溶蛋白基因Tagli-γ-ll的克隆及其互作蛋白质分析

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中图分类号：S512.1;Q756 文献标识码：A 文章编号： 1000-4440（2025）05-0833-07

Abstract：To further analyze the regulation mechanism of γ -gliadingeneinflourqualityofwheat，the Tagli-y-11 gene wassucesfullycloned from Zhengmai158（low proteincontent and high dough strength）.Bioinformatic analysis revealed that this gene possessed the typical structural characteristicsof γ -gliadin，containing eight conserved cysteine residues.Aceliac disease（CD）epitope（PQQSFPQQQ）was identified withinrepeatdomainIof the Tagli-y-11 protein，

located at amino acid positions 133-141 . Using the yeast two-hybrid（Y2H）system，thecDNAlibraryofZhengmai 158 was screened，yielding eight candidate proteins potentiallyinteractingwithTagli- γ -11.These included cysteine protease，fructose-bisphosphatealdolase，cysteine-rich and transmembrane domain-containing protein1，（1，3： 1，4）-β-D-glucanase，auxinresponse factor 17-like （ARF17-like），cell number regulator 8-like （CNR8- like），ubiquitin-associated domain-containing protein

DSK2b，transcription factor PIF1-like.Therotation validationassays performedoncysteine-rich and transmembrane domain-containing protein1，fructose-bisphosphate aldolase，and （ 1，3：1，4） -β-D-glucanase confirmed physical interaction withTagli- γ -11.Based on these results，itwashypothesized that Tagli γ -11interacted with theseproteinsand participated in the synthesis and degradation of storage proteins （such as gliadin）and starch within wheat grains，as wellas inreproductive growth processes.

Key words： Triticum aestivum L.；Tagli- ⋅γ -11 gene；yeast two-hybrid system；rotation validation

醇溶蛋白约占小麦籽粒总贮藏蛋白的 40% ，是赋予面团独特黏弹性的关键组分[1]。（剩余10509字）