کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1980755 | 1061878 | 2009 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A histidine in the β-CASP domain of Artemis is critical for its full in vitro and in vivo functions
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: A histidine in the β-CASP domain of Artemis is critical for its full in vitro and in vivo functions A histidine in the β-CASP domain of Artemis is critical for its full in vitro and in vivo functions](/preview/png/1980755.png)
چکیده انگلیسی
Artemis is a key factor of the nonhomologous end-joining (NHEJ) pathway, which is critical for DNA double-strand break (DSB) repair in eukaryotic cells. It belongs to the β-CASP family of nucleases, forming a distinct group within the metallo-β-lactamase superfamily. Proteins of this group are specific for nucleic acids and contain an original domain, the β-CASP domain, which serves as a cap covering the active site displayed by the metallo-β-lactamase domain.Here, we have identified in the highly divergent sequences of the β-CASP domains from DNA-specific nucleases two conserved residues (Artemis E213 and H254), which are not present in RNA-specific enzymes, and shown that H254 plays a key role in the Artemis function, as it is critical for its full activity in vitro. Moreover, inherited mutation of H254 results in radiosensitive severe combined immune deficiency (RS-SCID) in humans. This residue might play a key role in specificity towards DNA, if not directly in zinc binding.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: DNA Repair - Volume 8, Issue 2, 1 February 2009, Pages 202-208
Journal: DNA Repair - Volume 8, Issue 2, 1 February 2009, Pages 202-208
نویسندگان
Jean-Pierre de Villartay, Noriko Shimazaki, Jean-Baptiste Charbonnier, Alain Fischer, Jean-Paul Mornon, Michael R. Lieber, Isabelle Callebaut,