Herbisit dayanıklılığını anlamak: Domates ve patatesteki AHAS (asetohidroksiasit sentetaz) genlerinin biyoinformatik analizleri

Yıl 2019, Cilt: 32 Sayı: 2, 201 - 210, 01.08.2019

Fırat Kurt

https://doi.org/10.29136/mediterranean.559688

Öz

Enzimlerin
mutasyon bölgelerinin belirlenmesi herbisitlere dayanıklı bitkilerin
yetiştirilmesi ve yabancı ot kontrol uygulamalarının başarısı için önemlidir.
Bu çalışma domates (SlAHAS) ve patatesteki (StAHAS) asetohidroksiasit sentetaz
(AHAS, EC
2.2.1.6) enzimlerine herbisit dayanıklılığını sağlayacak mutasyon bölgelerinin
biyoinformatik yöntemlerle belirlenmesi amacıyla yapılmıştır. AHAS proteinleri
evrimsel olarak yüksek oranda korunmasına rağmen bu proteinlerin uzunlukları
farklılık göstermektedir. SlAHAS’ta Lys541 ve Val542 amino asitleri (aa) enzim aktivitesi için
önem taşımaktadır ve Lys541 Ala, Phe, Arg, ve Val aa ile yer değiştirebilirken;
Ile sadece Val542 ile yer değiştirebilir aa olarak bulunmuştur. Benzer şekilde
StAHAS’ta Ile124, Met266 ve Leu272 stabilizasyonu sağlayacı aa olarak
bulunmuştur. Lys ve Arg, Ile124 ile değişebilir aa olarak saptanırken; Leu,
Met266 ile ve Ala, Pro ve Ser ise Leu272 ile enzim stabilizayonunu sağlayıcı
yer değiştirebilir aa olarak bulunmuştur. SlAHAS’taki kenetlenme analizlerine
göre klorosülfüron (CS) için Ser387, Arg235 ve His341; imazakin (IQ) içinse
Phe11, Ala40 ve His341 en yüksek bağlanma sonuçlarını vermiştir. StAHAS’ta ise
Lys232, Asn123 ve Arg53’ün CS ile bağlandığı; Lys405, Lys489 ve Arg268 ise IQ
ile bağlanabilecek aa’ler olduğu tespit edilmiştir. His341 ve Gln478’in CS ve
IQ ile SlAHAS’ta; Val61 ve Arg366’nın ise StAHAS’ta sırasıyla her iki ligand
ile bağ yapabildiği görülmüştür. Bunun yanısıra Arg366 SlAHAS’ta IQ ligantının
bağlanabileceği aa olarak bulunmuştur.

Anahtar Kelimeler

Asetohidroksiasit sentetaz, Asetolaktat sentetaz, Herbisit dayanıklılığı, Mutasyon

Insights into herbicide resistance: Bioinformatics analyses of AHAS (acetohydroxyacid synthase) genes in tomato and potato

Öz

The identification of enzymes’ mutable sites is important to the
development of herbicide resistant crops and for weed control practices. The
objective of this study was to provide insights into mutable residues causing
resistance to the acetohydroxyacid synthase enzyme (AHAS, EC 2.2.1.6) inhibitor
herbicides in the tomato (SlAHAS) and potato (StAHAS) through bioinformatics approaches.
The results showed AHAS proteins investigated in this study were highly
conserved but differed in length. Mutation analyses showed that Lys541 and
Val542 in SlAHAS were mutable sites for preservation of the enzyme activity.
While Ala, Phe, Arg, and Val residues were found to be substitutable with
Lys541, Ile was exchangeable for Val542. Similarly, Ile124, Met266, and Leu272
in StAHAS were identified as protein stabilizing residues. In this respect, Lys
and Arg were substitutable residues for Ile124, whereas Leu was for Met266 and
Ala, Pro and Ser were suitable residues for Leu272 regarding enzyme
stabilization. The docking analyses displayed that the best binding affinities
were obtained for Ser387, Arg235, and His341 for chlorosulfuron (CS) and Phe11,
Ala40, and His341 have the highest binding score for imazaquin (IQ) in SlAHAS.
As for StAHAS, Lys232, Asn123, and Arg53 residues were found to bind with CS
whereas Lys405, Lys489, and Arg268 amino acids were identified as sites where
IQ bound. His341 and Gln478 were binding residues for both CS and IQ in SlAHAS
whereas both ligands were found to bind with Val61 and Arg366 in StAHAS. Arg366
was identified as a binding site in SlAHAS for IQ as well.

Anahtar Kelimeler

Acetohydroxyacid synthase, Acetolactate synthase, Herbicide resistance, Mutation

Kaynakça

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