تجزیه و تحلیل بیوانفورماتیک خصوصیات فیزیکوشیمیایی، تغییرات پس‌ترجمه‌ای و دمینی ‏پروتئین‌های درگیر در تحمل شوری گندم ‏

نوع مقاله : علمی پژوهشی

نویسندگان

گروه به‌نژادی و بیوتکنولوژی گیاهی، دانشکده کشاورزی، ‏دانشگاه تبریز، تبریز، ایران.‏

چکیده

شوری یکی از مهم‌ترین تنش‌های محیطی است که باعث اختلال در رشد طبیعی گیاهان می‌شود. گیاه برای مقابله با شرایط تنش‌زا، از جمله تنش شوری مکانیسم‌های مختلفی را به کار می‌گیرد که از مهم‌ترین آنها در سطح مولکولی، تغییر در بیان پروتئین‌ها است. تغییر بیان پروتئین‌ها در گرو تغییرات فیزیکوشیمیایی آنها مثل نیمه عمر، شاخص پایداری، نقطه ایزوالکتریک، وزن مولکولی و ضریب خاموشی است. در این پژوهش تعدادی از پروتئین‌های دارای تغییر بیان تحت تنش شوری در گندم برای تجزیه و تحلیل‌های بیوانفورماتیکی استفاده شده است. از بین 25 پروتئین مرتبط با تنش شوری مورد مطالعه، تعداد 20 پروتئین دارای نیمه عمر بیشتر از 20 ساعت بودند. وزن مولکولی این پروتئین‌ها بین 13 تا 117 کیلو دالتون بوده و 15 پروتئین شاخص ناپایداری کمتر از 40 داشته و پایدار برآورد شدند. از بین پروتئین‌های درگیر در تنش شوری گندم α- توبولین به عنوان یک مونومر به همراه - توبولین در یک دایمر به نام α- توبولین شرکت می‌کند. توبولین، بخش عمده میکروتوبول‌ها را ایجاد می‌کند که برای رشد و تقسیم سلولی ضروری‌اند. این پروتئین دارای یک الگو به نامTubulin subunits alpha, beta and gamma signature و یک دمین به نام PLN00221 می‌باشد. برای پروتئین تریوزفسفات‌ایزومراز، دمینی با نام TIM- like beta/ alpha barrel domains که در مکانیسم کاتالیزوری نقش دارد و برای پروتئین کالمودولین یک دمین به نام PTZ00184 شناسایی شد که دمین متصل شونده به کلسیم می‌باشد. برای پروتئینPutative glycine decarboxylse subunit دمینی به نام PRK01202 شناسایی شد که فعالیت کربوکسیلازی دارد. برای پروتئین 2-Cys proxiredoxin BAS 1 دمین PRX- Typ 2 cys شناسایی شد که نقش مهمی در تنظیم اکسیداسیون- احیای سلولی دارد. این پژوهش نشان داد که تنش شوری طیف وسیعی از پروتئین‌های با ویژگی‌های فیزیکی و شیمیایی بسیار متفاوت از هم را در بر می‌گیرد و شامل پروتئین‌های با وزن مولکولی سنگین و سبک، پایدار و ناپایدار، دارای نیمه عمر طولانی و کوتاه و دارای نقطه ایزوالکتریک متفاوت از هم می‌شود.

کلیدواژه‌ها

موضوعات

عنوان مقاله [English]

Bioinformatic analysis of physicochemical properties, post-translational ‎modifications and domains of proteins involved in wheat salt tolerance

نویسندگان [English]

  • Arezoo Asl alizade
  • Mahmoud Toorchi
  • Ali Bandehhagh
Department of Plant Breeding and Biotechnology, Faculty of Agriculture, ‎University of Tabriz, Tabriz, Iran.
چکیده [English]

Salinity is one of the most important environmental stresses that disrupt the natural growth of plants. Plant use different mechanisms to cope with stress conditions, such as salinity, in which changes in protein expression is the most important one at molecular level. Changes in protein expression depends on their physicochemical changes such as half- life, stability index, iso-electric point, molecular weight, extinction coefficient etc. Furtermore, identification of motifs, patterns and protein domains make it possible to predict changes in the conformation, structure and proteins functions. In this research was selected a number of changed protein in expression under salinity stress in wheat based on the previous proteomic studies for further was selected bioinformatic analysis. Study Physicochemical properties of proteins by ProtParam software, identification of domains by InterProScan and CDD, identification patters for prediction of post translational modification by ScanProsite, similarity by Blast, alignment of similar proteins for identification of conserved block was performed by T-Coffee. Out of the 25 proteins associated with salinity stress, 20 proteins have a half-life more than 20 hours. The molecular weight of these proteins was varied between 13 to 117 kDa and 15 protein showed instability index of less than 40 and therefore classified as stable proteins. Investigation of proteins using TMHMM and Protscale softwares, it was found that Aquaporins, Plasma membrane intrinsic proteins, Plasma membrane ATPase and Rust resistance kinase Lr10 are highly hydrophobic proteins, whose major structure located inside the membranes. Out of 25 proteins, 8 proteins were selected and analyzed for identification of patterns, domains, structure and function. α-tubulin as a monomer participates with -tubulin to make α-tubulin dimer. Tubulin create a major part of microtubules that are essential for cell growth and division. This protein consisted of one pattern, Tubulin subunits alpha, beta and gamma signature domain namly PLN00221. For the Triosphosphate isomerase protein, a domain called TIM, which is involved in the catalytic mechanism and for the Calmodulin protein a domain called PTZ00184 was identified which is a calcium binding domain. For the Putative glycine decarbixylase subunit a domain called PRK01202 has been identified that has carboxylase activity. For Cu/Zn superoxide dismutase protein the domain called as SOD is involved in the absorption of superoxide. For Fructose-bisphosphate aldolase protein, the catalytic converter domain was identified as PLV02455 and for Hsp 70- Hsp 90 organizing protein, STI1 domain was identified with ATPase property. For the 2- Cys peroxiredoxin BAS 1 protein, for the PRX-Typ 2 cys domain that plays an important role in regulating oxidation- cell reduction.

کلیدواژه‌ها [English]

  • data bank
  • extinction coefficient
  • motif
  • pattern
  • transmembrane

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