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Journal Article

Structure and activity of the only human RNase T2.

MPS-Authors
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Hsiao,  H. H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

1563878.pdf
(Publisher version), 9MB

Supplementary Material (public)

1563873-Suppl.doc
(Supplementary material), 269KB

Citation

Thorn, A., Steinfeld, R., Ziegenbein, M., Grapp, M., Hsiao, H. H., Urlaub, H., et al. (2012). Structure and activity of the only human RNase T2. Nucleic Acids Research, 40(17), 8733-8742. doi:10.1093%2Fnar%2Fgks614.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-1935-4
Abstract
Mutations in the gene of human RNase T2 are associated with white matter disease of the human brain. Although brain abnormalities (bilateral temporal lobe cysts and multifocal white matter lesions) and clinical symptoms (psychomotor impairments, spasticity and epilepsy) are well characterized, the pathomechanism of RNase T2 deficiency remains unclear. RNase T2 is the only member of the Rh/T2/S family of acidic hydrolases in humans. In recent years, new functions such as tumor suppressing properties of RNase T2 have been reported that are independent of its catalytic activity. We determined the X-ray structure of human RNase T2 at 1.6 Å resolution. The α+β core fold shows high similarity to those of known T2 RNase structures from plants, while, in contrast, the external loop regions show distinct structural differences. The catalytic features of RNase T2 in presence of bivalent cations were analyzed and the structural consequences of known clinical mutations were investigated. Our data provide further insight into the function of human RNase T2 and may prove useful in understanding its mode of action independent of its enzymatic activity.