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The analysis of the nuclear localization signal of hepatocyte nuclear factor 1-α transcription factor Skip to content Tez Künye Durumu The analysis of the nuclear localization signal of hepatocyte nuclear factor 1-α transcription factor / Hepatocyte nükleer faktörü 1-α transkripsiyon faktörünün nükleer lokalizasyon sinyalinin araştırılması Yazar:FAREED MOHAMMED ALI FAREED FAREED Danışman: PROF. DR. BARBAROS NALBANTOĞLU ; DR. ÖĞR. ÜYESİ ÖZLEM YALÇIN ÇAPAN Yer Bilgisi: Yıldız Teknik Üniversitesi / Fen Bilimleri Enstitüsü / Kimya Ana Bilim Dalı / Kimya Bilim Dalı Konu:Biyokimya = Biochemistry ; Biyoloji = Biology ; Genetik = Genetics Dizin: Onaylandı Yüksek Lisans İngilizce 2018 83 s. MODY (Maturity onset of diabetes of youth) diyabetin tek gene bağlı bir alt grubu olup en sık görülen tipi MODY3’tür. MODY3 hastalarında pankreas, böbrek ve karaciğerde görevli transkripsiyon faktörü olan HNF1A geninde mutasyonlar tespit edilmiştir. Bu mutasyonlar proteinin DNA’ya bağlanmasını, transaktivasyon fonksiyonunu ya da hücre çekirdeğine lokalize olmasını etkilemektedirler. Önceki çalışmalarda mutant R271W ve S345Y HNF1A proteinlerinin hücre çekirdeğine lokalize olmalarının hasarlı olduğu tespit edilmiştir. Ancak bu hasarın moleküler mekanizması henüz aydınlatılmamıştır. İmportin α taşıma reseptör ailesi transkripsiyon faktörü gibi hücre çekirdeğinde görevli proteinlerin hücre çekirdeğine taşınmasından sorumludur. Bu proteinler kargo proteinlerine kargo proteinler üzerinde bulunan NLS (Nuclear localization signal) motifleri üzerinden bağlanmaktadır. Klasik NLS motifleri bazik amino asitler içermesine rağmen, klasik olmayan NLS motiflerinin de bulunduğu gösterilmiştir. İmportin α, amino asit ve fonksiyonel benzerlik olarak 3 alt gruba ayrılmaktadır. Şu ana kadar HNF1A proteini üzerinde belli bir import sinyal motifi rapor edilmemiş olsa da HNF1A proteini ile yapılan çalışmalarda klasik NLS bölgesi tanımına uyan 3 bölge (A, B ve C bölgeleri) olduğu gösterilmiştir. A bölgesi HNF1A proteininde 158-171 amino asitleri arası, B bölgesi 197-205 amino asitler arası ve C bölgesi 271-282 amino asitler arasında yer almaktadır. Ancak HNF1A’nın taşınmasından sorumlu importin α alt grubu ve diğer klasik olmayan NLS bölgeleri henüz rapor edilmemiştir. Yürütülen bu projenin ilk amacı, HNF1A transkripsiyon faktörünün hücre çekirdeğine taşınmasından sorumlu importin α alt grubunun tespit edilmesidir. Bu amaçla importin α proteinin 3 farklı alt grubu fare homolog karyopherin α proteinlerinden (Kpna2, 4 ve 6) seçilmiş ve seçilen proteinlerle HNF1A arasındaki etkileşim ko-immunoçöktüme yöntemiyle araştırılmıştır. Bu çalışma ile yabanıl HNF1A proteinin her 3 taşıyıcı protein ile de etkileşim halinde olduğu görülmüştür. En güçlü bağlanmayı Kpna6 proteini ile gösterdiğinden, projenin sonraki aşamalarında Kpna6 proteini ile devam edilmiştir. Bu etkileşimi doğrulamak için fare pankreas hücrelerinde (Min6) tespit edilen Kpna6 proteini siRNA kullanılarak susturulma çalışması yapılmış ve immunositokimyasal boyama çalışmasıyla HNF1A proteinin hücre içindeki lokalizasyonu araştırılmıştır. Kpna6 proteinin susturulması ile HNF1A’nın hücre çekirdeğine %10 daha az lokalize olduğu tespit edilmiştir. Projenin ikinci amacı ise MODY hastalarında tespit edilen ve hücre çekirdeğine lokalizasyonu hasarlı mutant HNF1A proteinleri (R271W ve S345Y) ve importin α alt grubu arasındaki etkileşimin araştırılmasıdır. R271W mutasyonu klasik NLS motifleri içerisinde olup, tespit edilen importin α alt grubunun HNF1A’yı tanıyıp bağlanma bölgesinde yer almaktadır. Bu sebeple R271W mutant HNF1Ave Kpna6 taşıyıcı protein arasındaki etkileşim ko-immunoçöktürme yöntemiyle araştırılmıştır. Yabanıl tip HNF1A ile karşılaştırıldığında R271W mutant HNF1A proteini ile Kpna6 proteini arasında daha az etkileşim olduğu görülmüştür. Bu sonuç R271W mutasyonunun proteinin klasik bir NLS motifi içerisinde yer aldığını doğrulamış oldu. S345Y mutant HNF1A proteini ise klasik bir NLS motifi içerisinde bulunmamasına rağmen, hücre çekirdeği lokalizasyonunda hasarlı olduğu tespit edilmiştir. Ko-immunoçöktürme çalışmalarında, bu mutant HNF1A proteinin, Kpna6 taşıyıcı protein ile etkileşiminde azalma gözlemlenmiş, bu da bu bölgenin klasik olmayan bir NLS bölgesi olduğunu desteklemektedir. Sonuç olarak yürütülen bu proje ile ilk defa HNF1A transkripsiyon faktörünün hücre çekirdeğine taşınma yolağında görevli taşıyıcı proteinler tespit edilmiş ve MODY3 hastalarında hastalığa sebep olan mutasyonların moleküler patogenezinin aydınlatılmasına katkı sağlamıştır. Ayrıca S345Y mutasyonun HNF1A proteinin üzerinde klasik olmayan NLS bölgesinde bulunduğu hipotezi de desteklenmiştir. Bu çalışmanın sonuçları, klasik olmayan NLS bölgeleri ile ilgili literatüre katkı sağlamış olacak ve daha detaylı projelerin hazırlanmasına önveri oluşturacaktır. Maturity-onset diabetes of the young (MODY) is a monogenic subtype of diabetes mellitus. MODY3 associated with HNF1A gene mutations is the most common form of MODY. HNF1A protein is a transcription factor which is expressed mainly in pancreas, liver and kidney. Functional characterization of HNF1A gene mutations revealed that they affect DNA binding, transactivation function and nuclear localization of HNF1A. In previous studies R271W and S345Y mutant HNF1A were found to be defective in nuclear localization, but molecular mechanisms of this transport defect was not clarified yet. Importin-α receptor family are responsible for translocating proteins such as transcription factors (HNF1A) into the nucleus. Importin proteins recognize and bind to nuclear localization signal (NLS) motifs which are found on cargo proteins. Although classic NLS motifs are known to consist of basic amino acids, non-classical NLS motifs were also reported. Importin α proteins are categorized into three groups based on the identity of amino acid sequence and function. To date, no single import signal in the HNF1A protein has been identified, but there are three regions that fit the description of an NLS: region A (amino acids 158-171), region B (amino acids 197-205) and region C (amino acids 271-282). However, importin α subtype which recognizes and binds to HNF1A has not been reported yet. One of the aims of this study is to identify the importin α subgroup which is responsible for the transport of HNF1A protein into the nucleus. For this purpose the interactions of HNF1A with three candidate importin α proteins were be evaluated by co-immunoprecipitation technique. In this study, homolog mouse karyopherin α proteins (Kpna2, 4 and 6) were used. The results of co-IP revealed that HNF1A protein is recognized and bound by all three importin α subgroup proteins. The strongest band was observed with Kpna6 protein, therefore in the following part of the experiment the interactions with Kpna6 protein were analyzed. To confirm this interaction, Kpna6 was knockdown by siRNA in mouse pancreatic cells (MIN6) and the location of HNF1A was analyzed by immunochemical staining techniques. The results showed that there is 10% reduction in the nuclear localization of HNF1A protein when the Kpna6 protein is silenced. Second purpose of the study was to analyze the interaction between predetermined importin α subgroup and mutant HNF1A proteins (R271W and S345Y) which were identified in MODY patients. R271W mutation resides in a region similar to classical NLS motif of HNF1A protein. Therefore, the interaction between mutant HNF1A and importin α will be evaluated by co-immunoprecipitation technique. A reduced interaction was observed when compared to the interaction with the wild type and this confirmed that R271W mutation resides in the classical NLS motif in HNF1A protein. S345Y mutation is on the other hand, does not reside in a classical NLS, but was shown to have nuclear localization defect in functional studies. A reduced interaction of S345Y mutant protein with Kpna6 protein was detected and this result showed that this region is a possible non-classical NLS motif in HNF1A protein. As a conclusion, the results of this study clarified the molecular pathway of nuclear import of HNF1A protein and molecular pathogenesis of HNF1A mutations in MODY3 patients. Also the identification of non-classical NLS motifs in HNF1A protein will contribute to the literature and also will provide a preliminary result for further projects.
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