Publications

Selected publications

• Antibiotic hyper-resistance in a class I aminoacyl-tRNA synthetase with altered active site signature motif.

Brkic A, Leibundgut M, Jablonska J, Zanki V, Car Z, Petrovic Perokovic V, Marsavelski A, Ban N, Gruic-Sovulj I. Nat Commun. 14 (2023):5498. doi: 10.1038/s41467-023-41244-3. https://www.nature.com/articles/s41467-023-41244-3

• Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases

Zivkovic I, Ivkovic K, Cvetesic N, Marsavelski A, Gruic-Sovulj I. Nucleic Acids Res. 50 (2022) 4029- 4041 https://academic.oup.com/nar/article/50/7/4029/6561661?login=true

• A pair of isoleucyl-tRNA synthetases in Bacilli fulfills complementary roles to keep fast translation and provide antibiotic resistance

Zanki V, Bozic B, Mocibob M, Ban N, Gruic-Sovulj I. Protein Sci. 31 (2022) e4418. doi: 10.1002/pro.4418. https://onlinelibrary.wiley.com/doi/10.1002/pro.4418

• How evolution shapes enzyme selectivity - lessons from aminoacyl-tRNA synthetases and other amino acid utilizing enzymes

Tawfik DS, Gruic-Sovulj I. FEBS J. 287 (2020) 1284-1305. https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.15199

All publications

• Resilience and proteome response of Escherichia coli to high levels of isoleucine mistranslation

Pranjic M, Spät P, Semanjski Curkovic M, Macek B, Gruic-Sovulj I,Mocibob M. Int J Biol Macromol. 262 (2024):130068. https://pubmed.ncbi.nlm.nih.gov/38340920/

• Kinetic characterization of amino acid activation by aminoacyl-tRNA synthetases using radiolabelled γ-\[32P]ATP

Živković I, Dulic M, Kozulic P, Mocibob M, Gruic-Sovulj I. FEBS Open Bio. 2024 https://febs.onlinelibrary.wiley.com/doi/10.1002/2211-5463.13903

• Exploring mechanisms of mupirocin resistance and hyper-resistance

Zivkovic I, Gruic-Sovulj I. Biochem Soc Trans. 52 (2024):1109-1120. https://pubmed.ncbi.nlm.nih.gov/38884776/

• Evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase are important for its resistance to oxidation.

Evic V, Soic R, Mocibob M, Kekez M, Houser J, Wimmerová M, Matković-Čalogović D, Gruic-Sovulj I, Kekez I, Rokov-Plavec J. FEBS Lett. 597 (2023), 2975-2992. https://pubmed.ncbi.nlm.nih.gov/37804069/

• Gly56 in the synthetic site of isoleucyl-tRNA synthetase confers specificity and maintains communication with the editing site

Dulic M, Krpan N, Gruic-Sovulj I. FEBS Lett. 597 (2023), 3114-3124. doi: 10.1002/1873- 3468.14780. https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14780

• Antibiotic hyper-resistance in a class I aminoacyl-tRNA synthetase with altered active site signature motif.

Brkic A, Leibundgut M, Jablonska J, Zanki V, Car Z, Petrovic Perokovic V, Marsavelski A, Ban N, Gruic-Sovulj I. Nat Commun. 14 (2023):5498. doi: 10.1038/s41467-023-41244-3. https://www.nature.com/articles/s41467-023-41244-3

• Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases

Zivkovic I, Ivkovic K, Cvetesic N, Marsavelski A, Gruic-Sovulj I. Nucleic Acids Res. 50 (2022) 4029- 4041 https://academic.oup.com/nar/article/50/7/4029/6561661?login=true

• A pair of isoleucyl-tRNA synthetases in Bacilli fulfills complementary roles to keep fast translation and provide antibiotic resistance

Zanki V, Bozic B, Mocibob M, Ban N, Gruic-Sovulj I. Protein Sci. 31 (2022) e4418. doi: 10.1002/pro.4418. https://onlinelibrary.wiley.com/doi/10.1002/pro.4418

• Uniform binding and negative catalysis at the origin of enzymes

Noor E, Flamholz AI, Jayaraman V, Ross BL, Cohen Y, Patrick WM, Gruic-Sovulj I, Tawfik DS. Protein Sci. 31 (2022) e4381. https://onlinelibrary.wiley.com/doi/10.1002/pro.4381

• Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip.

Pang L, Zanki V, Strelkov SV, Van Aerschot A, Gruic-Sovulj I, Weeks SD. Commun Biol. 5 (2022)

  1. https://www.nature.com/articles/s42003-022-03825-8
• The evolutionary history of the HUP domain

Gruic-Sovulj I,Longo LM, Jabłońska J, Tawfik DS. Crit Rev Biochem Mol Biol. 57 (2022) 1-15. https://www.tandfonline.com/doi/full/10.1080/10409238.2021.1957764

• Expression of genes for selected plant aminoacyl- tRNA synthetases in the abiotic stress

Baranašić, J; Mihalak, A, Gruic-Sovulj, I, Bauer, N, Rokov Plavec, J. Acta botanica Croatica, 80 (2021) 35-42 https://hrcak.srce.hr/243653

• Mechanism of discrimination of isoleucyl-tRNA synthetase against nonproteinogenic α-aminobutyrate and its fluorinated analogues

Zivkovic I, Moschner J, Koksch B, Gruic-Sovulj I. FEBS J. 287 (2020) 800-813. https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.15053

• Polyamines Mediate Folding of Primordial Hyperacidic Helical Proteins

Despotović D, Longo LM, Aharon E, Kahana A, Scherf T, Gruic-Sovulj I, Tawfik DS. Biochemistry. 59 (2020) 4456-4462. https://pmc.ncbi.nlm.nih.gov/articles/PMC7735664/

• How evolution shapes enzyme selectivity - lessons from aminoacyl-tRNA synthetases and other amino acid utilizing enzymes

Tawfik DS, Gruic-Sovulj I. FEBS J. 287 (2020) 1284-1305. https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.15199

• On the Mechanism and Origin of Isoleucyl-tRNA Synthetase Editing against Norvaline

Bilus M, Semanjski M, Mocibob M, Zivkovic I, Cvetesic N, Tawfik DS, Toth-Petroczy A, Macek B, Gruic-Sovulj I. J Mol Biol. 431 (2019) 1284-1297 https://pubmed.ncbi.nlm.nih.gov/30711543/

• Arabidopsis seryl-tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl-tRNA synthetase

Kekez M, Zanki V, Kekez I, Baranasic J, Hodnik V, Duchêne AM, Anderluh G, Gruic-Sovulj I, Matković-Čalogović D, Weygand-Durasevic I, Rokov-Plavec J. FEBS J. 286 (2019) 536-554 https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.14735

• An archaeal aminoacyl-tRNA synthetase complex for improved substrate quality control

Crnković A, Čavužić M, Godinić-Mikulčić V, Anderluh G, Weygand-Đurašević I, Gruic-Sovulj I. Biochimie. 147 (2018) 36-45. https://pubmed.ncbi.nlm.nih.gov/29273296/

• Kinetic Origin of Substrate Specificity in Post-Transfer Editing by Leucyl-tRNA Synthetase

Dulic M, Cvetesic N, Zivkovic I, Palencia A, Cusack S, Bertosa B, Gruic-Sovulj I. J Mol Biol. 430 (2018) 1–16 - Featured article, Ibba & Kelly, J Mol Biol. 430 (2018) 17–19 https://pubmed.ncbi.nlm.nih.gov/29111343/

• Discovery and Investigation of Natural Editing Function against Artificial Amino Acids in Protein Translation

Völler JS, Dulic M, Gerling-Driessen UI, Biava H, Baumann T, Budisa N, Gruic-Sovulj I, Koksch B.I ACS Cent Sci. 3 (2017) 73-80. https://pubs.acs.org/doi/10.1021/acscentsci.6b00339

• Synthetic and editing reactions of aminoacyl-tRNA synthetases using cognate and non-cognate amino acid substrates

Cvetesic N, Gruic-Sovulj I. Methods 113 (2017) 13-26. https://pubmed.ncbi.nlm.nih.gov/27713080/

• Naturally Ocurring Isoleucyl-tRNA-synthetase without tRNA-Dependent Pre-Transfer Editing

Cvetesic N, Dulic M, Bilus M, Sostaric N, Lenhard B, Gruic-Sovulj I. J Biol Chem 291 (2016) 8618-31 https://pmc.ncbi.nlm.nih.gov/articles/PMC4861432/

• Seryl-tRNA Synthetases in Translation and Beyond

Močibob M, Rokov-Plavec J, Godinić- Mikulčić V, Gruić-Sovulj I. Croat Chem Acta 89 (2016) 261- 276 https://hrcak.srce.hr/168001

• Proteome-wide measurement of non-canonical bacterial mistranslation by unbiased quantitative mass spectrometry of protein modifications

Cvetesic N, Semanjski M, Soufi B, Krug K, Gruic-Sovulj I,Macek B. Sci Rep 6 (2016) 28631. https://www.nature.com/articles/srep28631

• The tRNA A76 hydroxyl groups control partitioning of the tRNA-dependent pre- and post-transfer editing pathways in class I tRNA synthetase

Cvetesic N, Bilus M, Gruic-Sovulj I. J Biol Chem 290 (2015) 13981. https://www.sciencedirect.com/science/article/pii/S0021925818809061?via%3Dihub

• The origin of specificity and insight into recognition between an aminoacyl carrier protein and its partner ligase

Maršavelski A*,* Močibob M, Gruić-Sovulj I, Vianello R. Phys Chem Chem Phys. 17 (2015) 19030-8.

• Determinants for tRNA-dependent pretransfer editing in the synthetic site of isoleucyl- tRNA synthetase

Dulic M, Perona JJ, Gruic-Sovulj I. Biochemistry 53 (2014) 6189-98. https://pubmed.ncbi.nlm.nih.gov/25207837/

• Synthetic and editing mechanisms of aminoacyl-tRNA synthetases.

Perona JJ, Gruic-Sovulj I. Top Curr Chem. 344 (2014) 1-41. https://pubmed.ncbi.nlm.nih.gov/23852030/

• The physiological target for LeuRS translational quality control is norvaline

Cvetesic N, Palencia A, Halasz I, Cusack S, Gruic-Sovulj I. EMBO J. 33 (2014) 1639-53. – commentary Ribas de Pouplana L. EMBO J. 33 (2014) 1619-20 https://www.embopress.org/doi/full/10.15252/embj.201488199

• Lack of discrimination against non-proteinogenic amino acid norvaline by elongation factor Tu from Escherichia coli

Cvetesic N, Akmacic I, Gruic-Sovulj I. Croat Chem Acta. 86 (2013) 73-82. https://pmc.ncbi.nlm.nih.gov/articles/PMC3675784/

• Substrate recognition and fidelity of maize seryl-tRNA synthetases

Rokov-Plavec J, Lesjak S, Gruic-Sovulj I, Mocibob M, Dulic M, Weygand-Durasevic I. Arch Biochem Biophys 529 (2013) 122-30. https://pubmed.ncbi.nlm.nih.gov/23228595/

• Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps

Cvetesic N, Perona JJ, Gruic-Sovulj I. J Biol Chem 287 (2012) 25381-94. https://www.sciencedirect.com/science/article/pii/S0021925820737038?via%3Dihub

• An idiosyncratic serine ordering loop in methanogen seryl-tRNA synthetases guides substrates through seryl-tRNA Ser formation

Dulic M, Pozar J, Bilokapic S, Weygand-Durasevic I, Gruic-Sovulj I. Biochimie 93 (2011) 1761-1769. https://pubmed.ncbi.nlm.nih.gov/21704670/

• Pre-transfer editing of serine hydroxamate within the active site of methanogenic-type seryl-tRNA synthetase

Gruic-Sovulj I, Dulic M, Weygand-Durasevic I. Croat. Chem. Acta 84 (2011) 179–184. https://hrcak.srce.hr/71980

• Partitioning of tRNA-dependent Editing Between Pre- and Post-transfer Pathways in Class I Aminoacyl-tRNA Synthetases

Dulic M, Cvetesic N, Perona JJ, Gruic-Sovulj I. J. Biol. Chem. 285 (2010) 23799-23809. https://pmc.ncbi.nlm.nih.gov/articles/PMC2911327/

• Efficiently activated serine analogue is not transferred to yeast tRNA Ser

Gruic-Sovulj I, Dulic M, Jaric J, Cvetesic N, Majsec K, Weygand-Durasevic I. Croat. Chem. Acta 83 (2010) 163-169. https://hrcak.srce.hr/56019

• Differences between reversible (self-association) and irreversible aggregation of rHuG-CSF in carbohydrate and polyol formulations

Pavišic R, Dodig I, Horvatić A, Mijić L, Sedić M, Linarić Rajić M, Gruic-Sovulj I, Preočanin T, Bukvić Krajačić M, Cindrić M. European Journal of Pharmaceutics and Biopharmaceutics 76 (2010) 357–365. https://pubmed.ncbi.nlm.nih.gov/20854908/

• Synthesis and Biological Activity of Mannose Conjugates with 1-Adamantamine and Ferrocene Amines

Ribić R, Kovačević M, Petrović-Peroković V, Gruić-Sovulj I, Rapić V, Tomić-Pisarović S. Croat. Chem. Acta 83 (2010) 421-431.https://hrcak.srce.hr/62647

• Hydrolysis of non-cognate aminoacyl adenylates by a class II aminoacyl-tRNA synthetase lacking an editing domain

Gruic-Sovulj I, Rokov-Plavec J, Weygand-Đurašević I. FEBS Letters 581 (2007) 5110-5114. https://febs.onlinelibrary.wiley.com/doi/10.1016/j.febslet.2007.09.058

• Structure of the unusual seryl-tRNA synthetase reveals a distinct zinc-dependent mode of substrate recognition

Bilokapić S, Maier T, Ahel D, Gruic-Sovulj I, Söll D, Weygand-Đurašević I, Ban N. EMBO J. 25 (2006) 2498-509. https://www.embopress.org/doi/full/10.1038/sj.emboj.7601129

• Shuffling of discrete tRNA Ser regions reveals differently utilized identity elements in yeast and methanogenic archaea

Gruic-Sovulj I, Jarić J, Dulić M, Cindrić M, Weygand-Đurašević I. J. Mol. Biol. 361 (2006) 128-39 https://pubmed.ncbi.nlm.nih.gov/16822522/

• Amino acid-dependent transfer RNA affinity in a class aminoacyl-tRNA synthetase

Uter N, Gruic-Sovulj I, Perona JJ. J. Biol. Chem. 280 (2005) 23966-23977 https://www.sciencedirect.com/science/article/pii/S0021925820674543?via%3Dihub

• tRNA-dependent aminoacyl adenylate hydrolysis by a non-editing class I aminoacyl- tRNA synthetase

Gruic-Sovulj I, Uter N, Bullock T, Perona JJ. J. Biol. Chem. 280 (2005) 23978-23986 https://www.sciencedirect.com/science/article/pii/S0021925820674555?via%3Dihub

• Unilateral flexibility in tRNA Ser recognition by heterologous seryl-tRNA synthetase

Rokov Plavec J, Bilokapić S, Gruic-Sovulj I, Močibob M, Glavan F, Brgles M, Weygand-Đurašević I. Period. Biol. 106 (2004) 147-154

• Stability of the Complex Between Yeast Seryl-tRNA Synthetase and tRNA Ser under Different Electrophoretic Conditions

Gruic-Sovulj I, Rokov-Plavec J, Močibob M, Kamenski T, Weygand-Đurašević I. Croat. Chem. Acta 77 (2004) 599-604 https://hrcak.srce.hr/clanak/151549

• tRNA-dependent amino acid discrimination by yeast seryl-tRNA-synthetase

Gruic-Sovulj I, Landeka I, Söll D, Weygand-Đurašević I. Eur. J. Biochem. 269 (2002) 5271-5279.

• The accuracy of seryl-tRNA synthesis

Weygand-Đurašević I, Gruic-Sovulj I, Ročak S, Landeka I. Food Technol. Biotechnol. 40 (2002) 247-253. https://hrcak.srce.hr/clanak/263153

• Influence of modified tRNA Tyr on the activation of tyrosine catalyzed by tyrosyl-tRNA synthetase from Saccharomyces cerevisiae

Gruic-Sovulj I, Weygand-Đurašević I, Kućan Ž. Croat. Chem. Acta 74 (2001) 161-171. https://hrcak.srce.hr/131785

• Detection of Noncovalent tRNA•Aminoacyl-tRNA Synthetase Complexes By Matrix- assisted Laser Desorption/Ionization Mass Spectrometry

Gruic-Sovulj I, Lüdemann H-C, Hillenkamp F, Weygand-Đurašević I, Kućan Ž, Peter-Katalinić J. Biol. Chem. 272 (1997) 32084-32091. https://www.sciencedirect.com/science/article/pii/S0021925818397333?via%3Dihub

• Matrix-assisted laser desorption/ionisation mass spectrometry of transfer ribonucleic acids isolated from yeast

Gruic-Sovulj I, Lüdemann H-C, Hillenkamp F, Weygand-Đurašević I, Kućan Ž, Peter-Katalinić J. Nucleic Acids Res. 25 (1997) 1859-1861. https://academic.oup.com/nar/article/25/9/1859/2902313

• Serum paraoxonase and cholinesterase activities in demented eldery patients

Reiner E, Hodoba D, Pavković E, Pecotić Z, Gruić I, Čović-Peko I, Simeon-Rudolf V. Period. Biol. 97 (1995) 301-304.

GRUIC-SOVULJ LAB
PROTEIN SYNTHESIS GROUP

Division of Biochemistry
Department of Chemistry
Faculty of Science
University of Zagreb
Horvatovac 102a, 10000 Zagreb, Croatia