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Biomolecules, Volume 9, Issue 3

March 2019 - 37 articles

Cover Story: Parvulin 42 (TbPar42) of Trypanosoma brucei plays a key role in cell growth. Knockdown of this nuclear protein in procyclic cells inhibits proliferation of the parasite. Orthologous proteins of TbPar42 are exclusively found in unicellular organisms and exhibit two-domains, an N-terminal forkhead-associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain. We used NMR spectroscopy and X-ray analysis to determine the structures of the isolated domains of TbPar42. We demonstrate the recognition of phosphorylated peptides by motifs within the FHA domain, and test the catalytic activity of the PPIase domain against a broad variety of substrates. The FHA domain of TbPar42 shows structural homology to FHA domains of nuclear RNA-binding proteins in multi-cellular organisms, suggesting a role of TbPar42 in RNA binding/processing. View this paper.
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Biomolecules - ISSN 2218-273X
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