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Investigating the residues that are responsible for pH dependent activity of the atpase domain of DNAK Skip to content Tez Künye Durumu Investigating the residues that are responsible for pH dependent activity of the atpase domain of DNAK / DNAK nın atpaz domaininin pH bağımlı aktivitesinden sorumlu amino asitlerin araştırılması Yazar:UMUT GÜNSEL Danışman: DOÇ. DR. GİZEM DİNLER DOĞANAY Yer Bilgisi: İstanbul Teknik Üniversitesi / Fen Bilimleri Enstitüsü / İleri Teknolojiler Ana Bilim Dalı / Moleküler Biyoloji-Genetik ve Biyoteknoloji Bilim Dalı Konu:Biyofizik = Biophysics ; Biyoloji = Biology ; Genetik = Genetics Dizin: Onaylandı Yüksek Lisans İngilizce 2013 74 s. Arkeadan ökaryotlara kadar bütün organizmalar kendi içsel dengelerini korumak için pH, sıcaklık değişimleri, oksidatif ve kimyasal stresler gibi çevresel durumlara cevap verirler. Bu tür durumlarda, belli bir grup proteinin ifadesi artarak bu içsel dengeyi sağlar. Bu proteinlere moleküler şaperon adı verilmektedir. Moleküler şaperonların hücre içerisinde vazgeçilmez görevleri vardır; yeni sentezlenen proteinlerin işlenmesi, proteinlerin organel membranlarından geçirilmesi, oligomerik proteinlerin alt birimlerine ayrılması, proteozom sisteminin asiste edilmesi ve bazı transkripsiyon faktörlerinin aktivitesinin düzenlenmesi gibi. Hsp70 proteinleri en yaygın bulunan proteinlerden olup bütün organizmaların sitoplazmasında ve ökaryotların neredeyse bütün organellerinde (endoplazmik retikulum, mitokondri, kloroplast vb…) bulunur. Hsp70 proteinleri görevlerini gerçekleştirirlerken ATP?yi döngüler halinde kullanırlar ve substrat bağlama bölgeleri ile substrata bağlanırlar. Burada substrat olarak belirtilen amino asit sekanslarındaki kısa hidrofobik bölgelerdir. Hsp70?ler diğer moleküler şaperonlar ile birlikte doğru katlanmamış, bozulmuş veya sentezlenmekte olan proteinlerin doğru katlanma yollarına yönlenmesini sağlarlar. Enzimlerde olduğu gibi doğru katlanma reaksiyonunu hızlandırmazlar. Yaptıkları tek şey bu hidrofobik bölgelerin istenmeyen bir şekilde birbirleri ile ilişki kurmasını engellemektir. Hsp70 proteinleri 44 kDa?lık N-terminal nükleotid bağlama domeni (NBD), 25 kDa?lık C-terminal substrat bağlama domeni (SBD) ve bu domenleri birbirine bağlayan oldukça korunmuş, kısmen hidrofobik bir bağlaçtan oluşur. SBD substrat moleküllerine afinite gösterirken; NBD, SBD?nin substrata olan ilgisini bağlaç aracılığıyla kontrol eder. Oluşturulan farklı nükleotit bağlı konformasyonlar farklı substrat afinitesine sahip olmaktadır. NBD?ye ATP bağlandığında bağlaç bölgesi NBD?nin lobları arasındaki hidrofobik yarığa girer ve iki domenin yapışık olmasını sağlar. Bu durumda SBD?nin kapağı açılır ve substrat afinitesi düşer. Diğer bir deyişle substrat bağlanma/ayrılma (kon/off) kinetiği artar. ATP?nin ADP?ye hidrolizi ise hidrofobik yarığın kapanmasına ve iki domenin ayrılmasına neden olur. SBD?nin kapağı kapanır ve substrat afinitesi artar. Yani substrat bağlanma/ayrılma kinetiği azalır. NBD?nin farklı nükleotit durumlarıyla SBD?yi kontrol etmesinin yanı sıra; SBD?ye substrat bağlanması da NBD?nin ATPaz hızını arttırmaktadır. Domenler arası kurulan bu karşılıklı, allosterik kominikasyonda, evrimsel olarak oldukça korunmuş 388VLLL392 bağlaç sekansının önemli bir rol aldığı bilinmektedir. Kesilmiş DnaK proteinleri, 389VLLL392 sekansını içeren [DnaK(1-392)] ve içermeyen [DnaK(1-388)], ile yapılan ATPaz ölçümleri bu rolün önemini açıkça göstermiştir. 389VLLL392 sekansını içermeyen NBD, tam dizilim DnaK?nın [DnaK(1-638)] ortamda susbtrat bulunmadığında gösterdiği aktiviteye benzer bir eğriye sahip olurken; 389VLLL392 sekansını içeren NBD, tam dizilim DnaK?nın substrat ile stimüle olmuş pH bağımlı aktivitesine benzer bir aktivite sergilemektedir. NBD de kendi içerisinde I ve II olmak üzere iki loba ve her lob da A ve B olmak üzere iki altdomene ayrılır. Lob-I ve lob-II arasında nükleotit bağlama bölgesini sararken, IA ve IIA altdomenleri arasında hidrofobik bağlaç bağlanma yarığı oluşur. Nükleotit bağlanma bölgesinde ADP bağlı durumda: E267, K270 ve S274 nükleotitin adenozin kısmıyla; G442?nin amid grubu ?-fosfat ile; ve T11, T12 ve N15?in omurga ve yan zinciri ß-fosfat ile ilişki halindedir. Ayrıca D8, D194 ve E171 magnezyum iyonunun ilk koordinasyon kabuğundaki sular ile ilişkilidir. Bu ilişkiler proteinin ADP?ye olan ilgisini büyük ölçüde belirlemektedir ve katalitik aktivitede önemli olabilirler. Bir önceki paragrafta da belirtildiği gibi farklı nükleotit bağlı durumlar farklı NBD konformasyonlarına neden olmaktadır. ATP bağlı NBD?de loblar arası etkileşimler daha fazladır ve nükleotit bağlanma bölgesi kapalıdır. İki lob birbirine ATP?nin yarattığı köprü ile bağlıdır. ATP hidrolizi gerçekleştiğinde ise bu köprü kırılır ve IIB altdomeni 200?lik bir açı ile döner. Böylece açık NBD konformasyonu oluşturulmuş olur. NBD açık konformasyona sahip olduğunda (Nükleotitsiz ve ADP bağlı konformasyon) IA ve IIA altdomeni arasında bulunan hidrofobik bağlaç bağlanma bölgesi kapalıdır. NBD kapalı konformasyona sahip olduğunda (ATP bağlı konformasyon) ise bu bölge açıktır ve domenler arası etkileşime izin verir. Sonuç olarak NBD?ye bağlanan nükleotit NBD?nin içsel konformasyonunu belirleyerek DnaK?nın substrat bağlama döngülerini gerçekleştirmesini sağlar. NBD?de gerçekleşen ATP hidroliz reaksiyonunun ise tam olarak nasıl gerçekleştiği bilinmemektedir. Bu konuda ATP hidroliz mekanizması bilinen proteinlere dayanarak çeşitli hipotezler ortaya atılmıştır ama henüz hiçbiri kesin olarak ispatlanamamıştır. SBD ise ß altdomeni ve ? altdomeni olmak üzere iki parçadan oluşur. ß altdomeni substratın bağlanmasına yataklık ederken (L1,2 ve L3,4 bölgelerinin arası), ? altdomeni bir kapak görevi görerek hidrofobik substratın üzerine kapanır (heliks A ve B) ve substratın hidrofilik ortamdan uzaklaştırılmasını sağlar. Heliks B ile ß altdomeni arasındaki bağlantı bir tuz köprüsü ve L3,4 ve L5,6 bölgeleri ile yapılan iki hidrojen bağı sayesinde kurulur. Heliks A ve B?nin aksine ? altdomenini oluşturan diğer helikslerin (C-terminal ucundaki C, D ve E heliksleri) rolü net bir şekilde anlaşılamasa da, yüksek sıcaklıklarda bu helikslerin ? altdomenini stabilize ettiği bulunmuştur. Bütün bu verilere rağmen Hsp70?lerin çalışma mekanizması şu ana kadar kesin bir biçimde ortaya koyulamasa da, allosterik ilişkiyi gösteren sonuçlar açıktır. Bunlara ek olarak yukarıda da belirtildiği gibi NBD?de gerçekleşen ATP hidrolizi reaksiyonunun da tam olarak nasıl gerçekleştiği bilinmemektedir. Daha önce yapılan çalışmalarda hidrolizde önemli olabilecek bazı amino asitlere dikkat çekilmiştir. Fakat yine de tatmin edici sonuçlar elde edilememiştir. Bu çalışmalardan biri T199?u bir otofosrilasyon bölgesi olarak belirtmekte ve T199?u olmazsa olmaz bir amino asit olarak tanımlamaktadır. Fakat daha sonra kesilmiş NBD ile yapılan deneylerde bu amino asitin ATP hidrolizi için vazgeçilmez olmadığı ortaya koyulmuştur. Başka bir çalışma proton kabul edicisi olarak aktif bölgede bulunan bazı asidik amino asitlere dikkat çekmiştir. E171, D201, D8 ve D194?ün mutasyonunun yapıldığı bu çalışmada ise ATP hidrolizinde sadece tek bir amino asitin proton kabul edicisi olarak görev almayabileceği ihtimali ortaya atılmıştır. Yine başka bir çalışmada K70 üzerine dikkatler çekilerek, bu amino asitin saldıracak nükleofil için bir pozisyonlandırıcı olabileceği ihtimali üzerinde durulmuştur. Biz de bu çalışmada yukarıda sözü edilen kesilmiş DnaK parçalarını kullandık. Bu projede aktivitenin pH bağımlılığından sorumlu olan amino asitleri araştırmak için, şüphelendiğimiz amino asitleri (D194 ve D201) site-directed mutagenez yöntemi ile alanin amino asitine çevirdik. Yaptığımız ATPaz aktivite, ADP-çıkış hızı ve stabilite deneyleri ile bu amino asitlerin aktivitede nasıl etkilere sahip olduğuna dair güçlü veriler elde etmiş bulunmaktayız. Deneysel çalışmalarımıza ek olarak yaptığımız hesapsal çalışmalar da elde ettiğimiz deneysel verileri desteklemektedir. Daha önceki çalışmalar ve bulunan kristal yapılar, D194?ün Mg2+?iyonunun ilk koordinasyon kabuğundaki sular ile etkileşerek, proteinin ATP afinitesini belirlediğini göstermiştir. Bizim çalışmalarımızda da, bu çalışmalarla tutarlı olarak, sözü edilen etkileşimlerin kaybolması sonucu nükleotit afinitesinin oldukça kaybolduğu bulunmuştur. Ayrıca hesapsal olarak bulunan pKa değerleri ile de D194?ün protonasyon durumunun proteinin aktivitesi için önemli olabileceği sonucu ortaya çıkmaktadır. Çalışmalarımızla D201 amino asitinin de bağlaç ile tetiklenen aktivitede sinyalizasyon yolağı üzerinde önemli bir role sahip olabileceği bulunmuştur. pH bağımlı deney sonuçlarımızla birlikte, stabilite ölçümlerimiz de bu sonucu desteklemektedir. Hsp70 proteins have essential roles in cells such as de novo folding of newly synthesized proteins, refolding or ubiquitination of denatured proteins, protein trafficking and translocation through membranes. In this project, we analyzed Escherichia coli DnaK which is the most investigated Hsp70 homolog. DnaK is comprised of an N-terminal nucleotide binding domain (NBD), a C-terminal substrate-binding domain (SBD) and a partially conserved hydrophobic linker that connects the domains. NBD is composed of two lobes (I and II) harboring the bound nucleotide and the lobes are also divided into two subdomains A and B. SBD is composed of an ?-helical lid and a ß-sandwich domain. It is clearly known that SBD has affinity to bind hydrophobic amino acid stretches in de novo or partially unfolded protein sequences. Its activity prevents the formation of unwanted inter and intra molecular hydrophobic interactions of proteins. NBD in the meantime can hydrolyze ATP molecules in order to control the activity of SBD. ATP binding to NBD causes the two domains to be docked, leading to the opening of the ?-helical lid. In this state, the affinity for substrate is low and the kon/off rate is high. On the other hand, in the ADP bound state two domains become separated and act like irrelevant beads bound with a flexible string. In this state, affinity for the substrate is high and kon/off rate is low as a result of the closure of the lid. Not only the nucleotide states of NBD controls the activity of SBD, but also binding of substrate enhances the ATPase rate indicating a reciprocal communication between the domains. Several studies showed that the communication is provided via the partially hydrophobic linker containing 389VLLL392 sequence. Investigations done with truncated DnaK constructs showed that presence or absence of this sequence as in the case of [DnaK(1-392)] and [DnaK(1-388)], respectively has specific features compared to that of the full-length protein [DnaK(1-638)]. It is proposed that the shorter construct has similar activity profile with the activity of the full-length protein in the absence of substrate which is at basal levels while the linker containing construct mimics the pH dependent activity of the substrate stimulated full-length protein. In this project we also used these constructs to investigate the allosteric signaling pathway in NBD. Here, we investigated residues D194 and D201 for the pH dependence of NBD and mutated them to alanine to see the effects of these residues. In addition to ATPase, ADP-dissociation and stability measurements, we also made molecular dynamic simulations to investigate the importance of D194 and D201. Our experimental data provide us strong evidence showing a relation of these residues with pH dependence, also pKa calculations using thermodynamic integration method supported our experimental data.
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