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TURAN, KADİR

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2018 - 201912020 - 20222
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    PublicationOpen Access
    Human sorting nexin 2 protein interacts with Influenza A virus PA protein and has a negative regulatory effect on the virus replication
    (SPRINGER, 2022-01) TURAN, KADİR; Kocmar, Tugba; Caglayan, Elif; Rayaman, Erkan; Nagata, Kyosuke; Turan, Kadir
    Background Replication of the influenza A viruses occurs in the cells through the viral RdRP consisting of PB1, PB2, and PA. Several cellular proteins are involved in these processes. This study aims to reveal the interaction between human SNX2 protein and the PA protein and the effects of the SNX2 on the virus replication. Results To identify potential host interacting proteins to the PA, yeast two-hybrid assay was carried out with HEK293 cell cDNA library and the PA as a bait. We focused on SNX2 protein, which interacts with the PA in the yeast cells. By using the co-immunoprecipitation assays, it has been demonstrated that the amino-terminal part of the PA was important for binding to the SNX2. Immunolocalization of the proteins in HeLa cells supported this interaction. Knockdown of the SNX2 with siRNA in the cells resulted in a significant increase in both viral transcripts and virus growth. However, the increase of SNX2 in transfected cells didn't cause a significant change in the viral RdRP activity in minireplicon assay. This may suggest that the negative effect of SNX2 on the virus replication could be saturated with its authentic intra-cellular amount. Conclusions This study revealed that the SNX2 and PA protein interact with each other in both yeast and HEK293 cells, and the SNX2 has a negative regulatory function on the virus replication. However, more knowledge is required to elucidate the action mechanism of the SNX2 on the influenza A virus replication at the molecular level.
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    PublicationOpen Access
    A SIMPLIFIED METHOD FOR THE EXTRACTION OF RECOMBINANT TAQ DNA POLYMERASE FROM ESCHERICHIA COLI
    (SLOVAK UNIV AGRICULTURE NITRA, 2018-04-01) TURAN, KADİR; Turan, Kadir; Eken, Burak
    DNA polymerase (Taq) enzyme isolated from Thermus aquaticus, a thermostable gram-negative bacterium, is a basic component of PCR, widely used in life sciences. The extraction and purification of this enzyme involves time-consuming and expensive steps such as precipitation of proteins with PEI and/or ammonium sulfate, column chromatography techniques, and removal of salts or other small molecular weight contaminants by dialysis. In this work, a novel and simplified method for extraction and purification of the recombinant Taq polymerase from Escherichia coli was employed, which used cold acetone instead of PEI or ammonium sulfate to precipitate the enzyme. The enzyme was efficiently recovered as active form from both the crude cell lysate and column fractions with cold acetone precipitation. This simplified method enabled us to obtain high quality Taq DNA polymerase in a much shorter time and at a lower cost.
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    PublicationOpen Access
    Human DDX56 protein interacts with influenza A virus NS1 protein and stimulates the virus replication
    (SOC BRASIL GENETICA, 2021) TURAN, KADİR; Pirincal, Aysegul; Turan, Kadir
    Influenza A viruses (IAV) are enveloped viruses carrying a single-stranded negative-sense RNA genome. Detection of host proteins having a relationship with IAV and revealing of the role of these proteins in the viral replication are of great importance in keeping IAV infections under control. Consequently, the importance of human DDX56, which is determined to be associated with a viral NS1 with a yeast two-hybrid assay, was investigated for IAV replication. The viral replication in knocked down cells for the DDX56 gene was evaluated. The NS1 was co-precipitated with the DDX56 protein in lysates of cells transiently expressing DDX56 and NS1 or infected with the viruses, showing that NS1 and DDX56 interact in mammalian cells. Viral NS1 showed a tendency to co-localize with DDX56 in the cells, transiently expressing both of these proteins, which supports the IP and two-hybrid assays results. The data obtained with in silico predictions supported the in vitro protein interaction results. The viral replication was significantly reduced in the DDX56-knockdown cells comparing with that in the control cells. In conclusion, human DDX56 protein interacts with the IAV NS1 protein in both yeast and mammalian cells and has a positive regulatory effect on IAV replication. However, the mechanism of DDX56 on IAV replication requires further elucidation.