| Title: | Full Professor |
| Function: | Head of Biochemistry Division |
| Location: | 303/ZBK |
| Public phone number: | +385 1 4606 230 |
| Internal phone number: | 6230 |
| E-mail: | |
| Department: | Division of Biochemistry |
undergraduate
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doctoral
Ita Gruić Sovulj was born in Zagreb, Croatia. She obtained her PhD in Chemistry/Biochemistry at the Department of Chemistry, Faculty of Science, University of Zagreb in 2001. As a NATO-NSF post-doctoral fellow, she joined Prof. Perona's group at the University of California at Santa Barbara, Santa Barbara, California, US, where she was trained in transient kinetic methods in enzymology (2003-2004). In 2005 she got an Assistant professorship position at the Department of Chemistry, Faculty of Science, University of Zagreb and started to build her research group. She was promoted to Associate professor in 2012 and to Professor in 2018.
Research in the Gruic group is focused on protein synthesis, specifically investigating aminoacyl-tRNA synthetases (aaRSs), the essential enzymes that link cognate amino acids and tRNAs for the ribosome. They explore how AARSs operate with high accuracy and how they are targeted by antibiotics. Additionally, they are studying error-correction (editing) mechanisms evolved by some AARS to cope with limits in initial discrimination against non-cognate amino acids. They also explore the cellular consequences of mistranslation and the role of editing in preventing the participation of non-proteinogenic amino acids in protein synthesis. AARSs are promising antibiotic targets, and they study mechanisms underlying resistance and hyper-resistance to the known antibiotics (such as mupirocin) and seek novel AARS inhibitors targeting microbials. For her scientific contribution, Ita Gruic was granted the National Science Award by the Republic of Croatia (Annual Science Award) in 2014.
Ita Gruic Sovulj is the Head of the Biochemistry Division of the Department of Chemistry, Faculty of Science, University of Zagreb and Head of the Biochemistry Field at the Doctoral Studies in Chemistry at the Faculty of Science. She was a Vice-dean for Science and Doctoral Studies at the Faculty of Science University of Zagreb (2018-2020). She is a Member of the Croatian Chemical Society, a Member of the Croatian Society for Biochemistry and Molecular Biology, Member of the editorial board of the journal Croatica Chemica Acta.
Note: this list of papers is located in an maintained by the Ruđer Bošković Institute which is in charge of the Croatian Scientific Bibliography Database (CROSBI). This link will take you to the appropriate CROSBI page of this person, containing a list of papers they have themselves entered in the database.
1. Zivkovic I, Gruic-Sovulj I. Exploring mechanisms of mupirocin resistance and hyper-resistance. Biochem Soc Trans. 52 (2024) 1109-1120.
2. Brkic A, Leibundgut M, Jablonska J, Zanki V, Car Z, Petrovic Perokovic V, Marsavelski A, Ban N, Gruic-Sovulj I. Antibiotic hyper-resistance in a class I aminoacyl-tRNA synthetase with altered active site signature motif. Nat Commun. 14 (2023), 5498.
3. Zanki V, Bozic B, Mocibob M, Ban N, Gruic-Sovulj I. A pair of isoleucyl-tRNA synthetases in Bacilli fulfills complementary roles to keep fast translation and provide antibiotic resistance. Protein Sci. 31 (2022) e4418.
4. Zivkovic I, Ivkovic K, Cvetesic N, Marsavelski A, Gruic-Sovulj I. Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases. Nucleic Acids Res. 50 (2022) 4029-4041.
5. Tawfik DS, Gruic-Sovulj I. How evolution shapes enzyme selectivity - lessons from aminoacyl-tRNA synthetases and other amino acid utilizing enzymes. FEBS J. 287 (2020) 1284-1305.
6. Bilus M, Semanjski M, Mocibob M, Zivkovic I, Cvetesic N, Tawfik DS, Toth-Petroczy A, Macek B, Gruic-Sovulj I. On the Mechanism and Origin of Isoleucyl-tRNA Synthetase Editing against Norvaline. J Mol Biol. 431 (2019) 1284-1297
7. Dulic M, Cvetesic N, Zivkovic I, Palencia A, Cusack S, Bertosa B, Gruic-Sovulj I. Kinetic Origin of Substrate Specificity in Post-Transfer Editing by Leucyl-tRNA Synthetase. J Mol Biol. 430 (2018) 1–16
8. Cvetesic N, Palencia A, Halasz I, Cusack S, Gruic-Sovulj I. The physiological target for LeuRS translational quality control is norvaline. EMBO J. 33 (2014) 1639-53
9. Cvetesic, N., Perona J.J., Gruic-Sovulj, I. Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps. J Biol Chem. 287 (2012) 25381-94.
10. Dulic, M., Cvetesic, N., Perona, J.J., Gruic-Sovulj, I. Partitioning of tRNA-dependent Editing Between Pre- and Post-transfer Pathways in Class I Aminoacyl-tRNA Synthetases. J. Biol. Chem. 285 (2010) 23799-23809.
2024-2028 Investigation of aminoacyl-tRNA synthetases as targets for antibiotics and how they develop resistance mechanisms (collaboration with Nenad Ban and Jeff Errington), Funding: Croatian Science Foundation and Swiss National Science Foundation
2019-2023 Investigation of substrate and editing specificity in tRNA synthetases and the mechanism of antibiotic action (collaboration with Nenad Ban and Dan Tawfik), Funding: Swiss National Science Foundation and Croatian Science Foundation
2017-2021 Aminoacyl-tRNA synthetases as gatekeepers of the standard genetic code, Funding: Croatian Science Foundation
2018-2020 Cellular responses to canonical and non-canonical mistranslation (collaboration with B. Maček), Funding: Ministry of Science and Education of the Republic of Croatia and DAAD
2014-2016 Role of translational quality control mechanisms in maintaining the functional Escherichia coli proteome (collaboration with B. Maček), Funding: Ministry of Science and Education of the Republic of Croatia and DAAD
2013-2016 Noncanonical roles of aminoacyl-tRNA synthetases, Funding: Croatian Science Foundation
2013-2015 The origin of amino acid specificity in editing class I aminoacyl-tRNA synthetases and cellular requirements for proofreading (collaboration with B. Lenhard and S. Cusack), Funding: Unity Through Knowledge Fund
2008-2011 Mechanism of proofreading by class I aminoacyl-tRNA synthetases (collaboration with J. Perona), Funding: NIH/FIRCA
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