Véronique Senty-Ségault's research while affiliated with University of Lorraine and other places

Publications (6)

Article
Full-text available
The U3 box C/D snoRNA is one key element of 90S pre-ribosome. It contains a 5΄ domain pairing with pre-rRNA and the U3B/C and U3C΄/D motifs for U3 packaging into a unique small nucleolar ribonucleoprotein particle (snoRNP). The RNA-binding protein Snu13/SNU13 nucleates on U3B/C the assembly of box C/D proteins Nop1p/FBL and Nop56p/NOP56, and the U3...
Article
Full-text available
In eukaryotes, U3 snoRNA is essential for pre-rRNA maturation. Its 5′-domain was found to form base pair interactions with the 18S and 5′-ETS parts of the pre-rRNA. In Xenopus laevis, two segments of U3 snoRNA form base-pair interactions with the 5′-ETS region and only one of them is essential to the maturation process. In Saccharomyces cerevisiae,...
Article
Full-text available
The eukaryal Snu13p/15.5K protein binds K-turn motifs in U4 snRNA and snoRNAs. Two Snu13p/15.5K molecules bind the nucleolar U3 snoRNA required for the early steps of preribosomal processing. Binding of one molecule on the C′/D motif allows association of proteins Nop1p, Nop56p, and Nop58p, whereas binding of the second molecule on the B/C motif al...
Article
The ribosomal L7Ae protein of archaea has the peculiarity to be a component of the C/D and H/ACA snRNPs, that guide rRNA post-transcriptional modifications. Its yeast (Snu13p) and human (15.5kDa protein) homologs are only found in C/D snoRNPs and the (U4/U6, U5) spliceosomal tri-snRNP. By using a large variety of RNAs, we compared the RNA-binding s...
Article
Full-text available
The 15.5-kD protein and its yeast homolog Snu13p bind U4 snRNA, U3 snoRNA, and the C/D box snoRNAs. In U4 snRNA, they associate with a helix-bulge-helix (K-turn) structure. U3 snoRNA contains two conserved pairs of boxes, C′/D and B/C, which were both expected to bind the 15.5-kD/Snu13 protein. Only binding to the B/C motif was experimentally demon...

Citations

... The FBL homolog in yeast, Nop1p, is also localized in the nucleolus and is involved in 18S rRNA processing and maturation. 26 Serum from patients with scleroderma, an autoimmune disease, often contains high levels of antibodies against FBL. 27 The exact mechanism by which FBL affects these processes has not been discovered, but some experimental data suggest that upregulation or downregulation of FBL can alter ribosomal structure and thus the relative translation efficiency of various mRNAs, potential contributing to the regulation of cell proliferation, cancer progression, and aging. ...
... rRNA maturation involves stepwise spacer cleavage from the polycistronic 45S pre-rRNA, which relies on extensive interactions between pre-rRNA and U3 RNA 37 . Several U3 binding sites on the 5′ external transcribed spacer (ETS) have been identified in bacteria and lower eukaryotes biochemically [38][39][40][41] , but the landscape of U3-pre-rRNA interactions within mammalian cells and how these interactions influence the 5′ ETS structure are unclear. The 5′ ETS of mammalian pre-rRNA harbors three closely located cleavage sites, namely A′, A0 and 1 (Fig. 4d) 37 . ...
... Описаны два основных класса мякРНК, различающиеся по содержащимся в них мотивам последовательностей нуклеотидов, структуре, взаимодействующим с ними белкам и, как следствие, химической модификации, которую они катализируют [119]. Малые ядрышковые РНК с C / D-боксами варьируются по длине от 70 до 130 нуклеотидов и характеризуются наличием сайтов C (RUGAUGA) и D (CUGA), обнаруженных около 5'-и 3'-концов молекулы и взаимодействующих посредством неканонического спаривания оснований, образующего кинк-поворот [120][121][122]. Дополнительные мотивы, C' и D', с такими же консенсусными последовательностями, как блоки C и D, соответственно, но часто менее консервативные, обнаруживаются в середине молекулы [118,122]. ...
... Our EMSA and SPR measurements show that the helical domain of g5Rp can bind with ssRNA with equally high affinity as the full-length protein. Six a-helices form a globin-fold-like helical domain, which is different from the traditional RNA binding domain that prefers to adopt the alpha/beta topologies (42)(43)(44)(45). According to the g5Rp structure, the surface electrostatic potential characteristics of the N terminus present a highly positively charged area on helix a5. ...
... This snoRNA is produced as individual transcription unit and is connected to the p53 pathway [88,89]. Although U3 includes C/D box-like motifs, it is not involved in 2 -O-Methylation of rRNA but rather is directing site-specific cleavage of rRNAs [90]. Moreover, the studies identified a robust snoRNA signature for both AITL and PTCL-NOS capable of classifying these patients depending on their outcome. ...