همسانه سازی cDNA و بررسی بیان ژن، خصوصیات فیزیک و شیمیایی و ساختارهای عملکردی آنزیم های بتاگالاکتوزیداز در میوه گوجه فرنگی

نوع مقاله : علمی - پژوهشی

نویسندگان

1 کارشناس ارشد گروه بیوتکنولوژی کشاورزی، دانشکده فنی و مهندسی، دانشگاه بین المللی امام خمینی(ره)، قزوین

2 استادیار بیوتکنولوژی کشاورزی، دانشکده فنی و مهندسی، دانشگاه بین‌المللی امام خمینی(ره)، قزوین

چکیده

بتاگالاکتوزیدازها در بسیاری از فرآیندهای مرتبط با رشدونمو گیاه شرکت نموده و به­عنوان آنزیم­های کلیدی در نرمی وابسته به رسیدگی میوه­های گوشتی معرفی شده­اند. در این مطالعه، طول کامل ششcDNA ی رمزکننده آنزیم­های بتاگالاکتوزیداز (نام­گذاری شده STBG2-7) از بافت میوه گوجه­فرنگی رقم فالکاتو (Falcato) همسانه­سازی و سطوح بیان و توالی اسیدآمینه مربوط به آنها بررسی گردیدند. با هم­ردیفی توالی­های پروتئینی منتج از STBG2-7، دو نیمه بسیار حفاظت­شده و کم حفاظت­شده در این آنزیم­ها شناسایی گردیده و براساس خصوصیات نیمه­های کم حفاظت­شده و یافته­های آزمایش­های اخیر پیشنهاد گردید که عملکردهای افتراقی این آیزوفرم­ها مرتبط با این نیمه­های کم حفاظت­شده می­باشند، که این نیمه­های کم حفاظت­شده با زیرواحدهای کوچک بتاگالاکتوزیدازهای هترودایمر متناظر می­باشند و با دو باقیمانده Trp و Glu کاملاً حفاظت­شده آغاز می­گردند.

کلیدواژه‌ها


عنوان مقاله [English]

cDNA Cloning and Investigating Gene Expression, Physicochemical Characteristics and Functional Structures of β-galactosidase Enzymes of Tomato Fruit (Lycopersicum esculentum cv. Falcato)

نویسندگان [English]

  • Alireza ghanad sabzevari 1
  • ramin hoseini 2
چکیده [English]

β-galactosidases participate in many processes related to plant development and are introduced as the key enzymes in the ripening-related softening of fleshy fruits. In this study, six full-length cDNAs encoding β-galactosidase enzymes (called STBG2-7) are cloned from the tomato fruit tissue of Falcato cultivar, and their expression levels and amino acid sequences are investigated. Also, the expression levels and amino acid sequences deduced from these isoforms are compared to their corresponding isoforms in Rutgers cultivar, and differences are studied and discussed. In the follow-up, by alignment of the protein sequences of STBG2-7, two highly-conserved and less-conserved halves are identified in these enzymes, and on the basis of the characteristics of the less-conserved halves and the recent experimental findings, it is suggested that the differential functions of these isoforms are related to these less-conserved halves.
 

کلیدواژه‌ها [English]

  • RT-PCR
  • Semi-quantitative PCR
  • Lectin domain
  • Protein
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