Beáta G. Vértessy, Chair of Board of the US-Hungarian Fulbright Foundation, signed agreement with Prof László Lovász, President of the Hungarian Academy of Sciences for joint support

The Hungarian Academy of Sciences, represented by its President, Professor László Lovász, and the Hungarian-American Fulbright Commission, represented by Board Chair Professor Beáta Vértessy and Károly Jókay, Executive Director, signed a multi-year agreement on March 23, 2016, in the the ornate concert hall in the Academy’s main building. Fulbright Board members Tamás MagyaricsTibor Frank and Eric Watnik (representing the US Embassy) also took part in the ceremony.

MTA Fulbright

The agreement will support Hungarian scholars who are employees of the Academy’s research network, on various “Momentum” (Lendület) teams, or are active in Academy-funded projects at Hungary’s universities. During the upcoming academic year 2016-17, two Hungarian researchers will be in the US on jointly-funded Fulbrights: one geophysicist and one astrophysicist. US scholars will also be eligible for the joint grants, and in 2016-17, one US sociologist will arrive in Budapest.

The Academy and Fulbright expect that up to 4 additional scholars per year will be able to conduct research in the US and in Hungary based on the terms of the agreement just signed.

For US scholars interested in applying for the 2017-18 Academic Year, see the CIES catalog of awards at:
catalog.cies.org

Hungarian researchers affiliated with the Academy please see:
www.fulbright.hu/fulbright-mta-kozos-osztondij

For further information contact the Fulbright Commission in Budapest at: This email address is being protected from spambots. You need JavaScript enabled to view it.

New paper published in Structural Chemistry

Our paper entitled "Exploring the role of the phage-specific insert of
bacteriophage Φ11 dUTPase" has been published in Structural Chemistry.

dUTPases are essential for maintaining genome integrity. Recently, in the case of a dUTPase from a Staphylococcal phage, another different physiological function was also suggested. Namely, it was shown that dUTPase from the Staphylococcus aureus bacteriophage Ф11 is capable of binding to the Staphylococcal Stl repressor protein. This binding interferes with the function of Stl. In the present study, we investigated the putative role of a phage dUTPase-specific peptide segment in the interaction of dUTPase with Stl and in impeding Stl–DNA complex formation. We show that dUTPase from Mycobacterium tuberculosis that lacks the phage-specific insert is also capable of disrupting the complexation between Stl and DNA. Hence, the insert segment is not essential for perturbation of the Stl function. However, we also demonstrate that in case of the phage dUTPase, the insert-lacking construct is deficient in perturbation of Stl activity. These findings clearly indicate that the phage-specific insert has a well-defined role only in the context of the phage dUTPase. Structural Chemistry, 30 August 2015, doi: 10.1007/s11224-015-0652-2

 

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