Mario Halic, PhD
Mario Halic, PhD

Mario Halic, PhD

Associate Member, St. Jude Faculty

Departments

Education

Diploma – University of Zagreb, Zagreb, Croatia (1999)
PhD – Humboldt University Berlin, Berlin, Germany (2005)
Postdoctoral Training – Harvard Medical School, Boston, USA

Honors & Awards

  • 2014  EMBO Young Investigator award
  • 2014  Cell 40 under 40 award
  • 2012  ERC starting grant
  • 2010   Charles King Trust Postdoctoral fellowship
  • 2007  EMBO Postdoctoral fellowship
  • 2006  Romer award, LMU Munich

Research Interests

Regulation of genome expression is essential for many cellular processes including cell proliferation, differentiation, development and viability. Heterochromatin, a silent fraction of chromatin, is essential to maintain genome stability and defects in heterochromatin formation lead to aberrant centromere and telomere function, aneuploidy and cancer. My group is focusing on molecular mechanism of recognition of repetitive and transposable genetic elements and epigenetic silencing by heterochromatin formation. We use genetics and genomics to decipher how genomes specify heterochromatic regions. We combine functional research with biochemistry and cryo-EM to study how heterochromatic proteins recognize and modify chromatin structure. This structural changes are necessary for heterochromatin formation and efficient silencing.

  • Recognition and silencing of foreign genetic elements
  • Chromatin modifications that lead to silencing (cryo-EM)
  • Changes in chromatin structure induced by chromatin modifiers (cryo-EM)

Halic Research Lab

Contact Information

Mario Halic, PhD Structural Biology MS 311, Room D5024E St. Jude Children’s Research Hospital 262 Danny Thomas Place Memphis, TN 38105-3678

St. Jude Faculty List

Related Topics

News Releases

Selected Publications

Bilokapic S, Suskiewicz MJ, Ahel I, Halic M. Bridging of DNA breaksactivate PARP2/HPF1 to modify chromatin. Nature 585(7826): 609-613, 2020.

Bilokapic S and Halic M. Nucleosome and ubiquitin position Set2 to methylate H3K36. Nat Commun 10(1):3795, 2019.

Ali-Ahmad A, Bilokapić S, Schäfer IB, Halic M*, Sekulić N*. CENP-C unwraps the human CENP-A nucleosome through the H2A C-terminal tail. EMBO Rep 20(10):e4891, 2019. (*corresponding authors)

Akoury E, Ma G, Demolin S, Broenner C, Zocco M, Cirilo A, Ivic N, Halic M. Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity. Nucleic Acids Res. 47(13): 6726-6736, 2019.

Ivic N, Potocnjak M, Solis-Mezarino V, Herzog F, Bilokapic S, Halic M. Fuzzy Interactions Form and Shape the Histone Transport Complex. Mol Cell 73(6): 1191-1203, 2019.

Bilokapic S, Strauss M, Halic M. Structural rearrangements of the histone octamer translocate DNA. Nat Commun Apr 6;9(1):1330, 2018.

Bilokapic S, Strauss M, Halic M. Histone octamer rearranges to adapt to DNA unwrapping. Nat Struct Mol Biol Jan;25(1):101-108, 2018.

Broenner C, Salvi L, Zocco M, Ugolini I, Halic M. Accumulation of RNAs on chromatin disrupts heterochromatin formation. Genome Res Jul;27(7):1174-1183, 2017.

Pisacane P, Halic M. Cid14 and Cid16 nucletidyltransferases recruit Rrp6 to degrade Argonaute-bound small RNAs and protect the genome from uncontrolled RNAi. Nat Comm May 25;8:15332, 2017.

Marasovic M, Zocco M, Halic M. Argonaute and Triman generate Dicer-independent priRNAs and mature siRNAs to initiate heterochromatin formation. Mol Cell Oct 24;52(2):173-83, 2013.

Gerace E, Halic M, Moazed D. The Methyltransferase Activity of Clr4Suv39h triggers RNAi Independently of Histone H3K9 Methylation. Mol Cell Aug 13;39(3):360-72, 2010.

Halic M, Moazed D. Dicer-Independent priRNAs and Argonaute Trigger RNAi and Heterochromatin Formation. Cell Feb 19;140(4):504-516, 2010.

Halic M, Blau M, Becker T, Mielke T, Pool MR, Wild K, Sinning I, Beckmann R. Following the Signal Sequence from the Ribosomal Tunnel Exit to Signal Recognition Particle. Nature Nov 23;444(7118):507-11, 2006.

Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R. Signal recognition particle receptor exposes the ribosomal translocon binding site. Science May 5;312(5774):745-7, 2006.

Halic M, Becker T, Frank J, Spahn CM, Beckmann R. Localization and dynamic behavior of ribosomal protein L30e. Nat Struct Mol Biol May;12(5):467-8, 2005. Epub 2005 May 1.

Halic M, Becker T, Pool MR, Spahn CM, Grassucci RA, Frank J, Beckmann R. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature Feb 26;427(6977):808-14, 2004.

Last update: March 2021

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