Ekmeklik Buğday Bitkisinden Ribozom İnaktivite Eden Proteinin (Tritin) in silico Analizi

Year 2022, Issue: 33, 79 - 87, 31.01.2022

Serap Demirel , Mustafa Usta , Abdullah Güller

https://doi.org/10.31590/ejosat.1021686

Cited By: 1

Abstract

Ribozom inaktive eden proteinler (RIP’ler) ribozomal RNA’da spesifik bir adeninin depürünasyonundan sonra protein sentezini baskılyan enzimlerdir. Tritin RIP ailesinden RNA-N glikosidaz domainine sahip tip I RIP’lerden biridir. Mevcut çalışmada Kutluk-94 buğday çeşidinin yapraklarından tritini kodlayan cDNA izole edildi ve pGEM-T Easy vektöre klonlandı. Recombinant plazmid sekanslandı. Farklı biyoinformatik araçlar tritin proteininin özelliklerinin değerlendirilmesi için kullanıldı. Bazı monokotil bitkilerde toplamda 38 tritin benzeri sekans tespit edildi. Sonuçlar tritin proteininin diğer RIP’lerde bulunan RNA N-glikozidaz aktivitesi ile ilişkili korunmuş domaine (Ricin-A) sahip olduğunu ortaya koydu. Çoklu sekans hizalamaya analizi tritinin RNA N-glikozidaz aktivitesinde hayati rol oynayan korunmuş amino asitlere sahip olduğunu göstermiştir. Bizim çalışmamızda in silico analizlerden elde edilen sonuçlar tritin proteinin moleküler ve yapısal özellikleri hakkında diğer araştırmacılara bilgi sağlayacaktır.

Keywords

Ribozom inaktive eden protein, tritin, cDNA

In silico Analysis of Ribosome-Inactivating Protein (Tritin) from Common Wheat Plants (Triticum aestivum L.)

Abstract

Ribosome-inactivating proteins (RIPs) are one of the enzymes that inhibit protein synthesis after depurination of a specific adenine in ribosomal RNA. The tritin is one of type I RIPs that include RNA-N glycosidase domain from RIP family. In the present study, cDNA encoding tritin from leaves of wheat Kutluk-94 cultivar was isolated and cloned into pGEM-T Easy vector. The recombinant plasmid was sequenced. The different bioinformatics tools were used for assessment of tritin protein characteristics. A total of 38 tritin-like sequences were identified in some monocot plants. Results showed that tritin protein have conserved domain (Ricin-A) found in other RIPs associated with RNA N-glycosidase activity and shows chancing homology to the RIPs in other plant species. According to multiple sequence alignment, tritin has conserved amino acids which are crucial role in RNA N-glycosidase activity. Our study illustrates that results obtained from in silico analyses could provide a perspective to another researcher about molecular and structural properties of tritin protein.

Keywords

Ribosome-inactivating protein, tritin, cDNA

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