In a girl, born of unrelated parents of European descent (family F), with Galloway-Mowat syndrome-10 (GAMOS10 619609), Arrondel et al. These findings suggested that YRDC may have additional functions besides being a member of the KEOPS complex. Patient cells showed increased susceptibility to genotoxic agents compared to controls, consistent with DNA repair defects. RNA sequencing of patient cells showed differential expression of genes involved in DNA damage response and repair. Q-FISH analysis in patient cells showed 26% telomere shortening of chromosomes compared to controls this was associated with increased cellular senescence. Patient fibroblasts showed normal YRDC protein levels and protein localization, but global t6A levels showed a significant decrease of 16.3% compared to wildtype. It was not present in the gnomAD database. The mutation, which was found by whole-exome sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. (2021) identified a homozygous missense mutation in the YRDC gene (I221T 612276.0004). In a male infant, born of distantly related Iraqi parents, with GAMOS10, Schmidt et al. These authors did not find alterations of telomere length in patient fibroblasts. Knockdown of YRDC in a human podocyte cell line resulted in decreased protein synthesis, decreased cell proliferation, and decreased cell survival. Studies of patient cells and in vitro studies in yeast showed that the mutations were unable to fully rescue growth defects and caused decreased t6A levels and lack of t6A modification. None were present in the gnomAD database. The mutations, which were found by whole-exome sequencing and confirmed by Sanger sequencing, segregated with the disorder in the families. (2019) identified homozygous or compound heterozygous hypomorphic or amorphic mutations in the YRDC gene ( 612276.0001- 612276.0003). In 3 patients from 2 unrelated families (families F and G) with Galloway-Mowat syndrome-10 (GAMOS10 619609), Arrondel et al. Subcellular fractionation and Western blot analysis localized Yrdc to the plasma membrane fraction of mouse kidney tissue. Northern blot analysis detected a 1.4-kb transcript in mouse tissues with strong expression in testis, thyroid, ovary, colon, kidney, and brain. The deduced 263-amino acid mouse protein has a calculated molecular mass of 27.8 kD. (2005) identified mouse Yrdc, which they called Irip. They identified YRDC transcripts of 1.9 and 1.2 kb that differ by alternate polyadenylation sites.īy differential display analysis of ischemia/reperfusion-treated mouse kidney RNA, Jiang et al. (2005) determined that YRDC has a calculated molecular mass of 28.3 kD. Northern blot analysis detected a 2.5-kb transcript in all human tissues examined with highest expression in liver, brain, and pancreas. YRDC shares 90% amino acid identity with its mouse ortholog and is highly conserved over its SUA5-YCIO-YRDC domain from E. The deduced 279-amino acid protein contains a SUA5-YCIO-YRDC domain, a GTP-binding elongation factor signature, and a leucine zipper motif. Using yeast 2-hybrid screening of a human fetal brain library with RBBP9 ( 602908) as bait, followed by EST database analysis and RACE, Chen et al.
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |