4 edition of Identification and characterization of a novel RNA-binding domain in SRM160 found in the catalog.
Identification and characterization of a novel RNA-binding domain in SRM160
John Alfred Leng Bowman
Thesis (M.Sc.) -- University of Toronto, 2001.
|Series||Canadian theses = -- Thèses canadiennes|
|The Physical Object|
|Pagination||1 microfiche : negative.|
We recently identified Rbm24 as a novel gene expressed during mouse cardiac development. Due to its tightly restricted and persistent expression from formation of the cardiac crescent onwards and later in forming vasculature we posited it to be a key player in cardiogenesis with additional roles in vasculogenesis and angiogenesis. To determine the role of this gene in cardiac development, we. Here, we present the identification of a novel S1 domain–containing protein and three unusually large ribosomal proteins, S2, S3, and S5, from the Chlamydomonas chloroplast small ribosomal subunit. Most of the other expected homologs of E. coli 30S subunit and a plastid-specific ribosomal protein were identified as well.
RNA-binding proteins' transcriptional and post-transcriptional regulation of RNA has a role in regulating the patterns of gene expression during development. Extensive research on the nematode C. elegans has identified RNA-binding proteins as essential factors during germline and early embryonic development. Their specific function involves the development of somatic tissues (neurons. The more extensive characterization of RNA binding by telomerase has included X-ray diffraction studies of the isolated RNA binding domain as well as the complete telomerase (18,32). Two regions of the protein appear to be involved in binding to the telomerase RNA.
The solution and crystal structures of the Nab2 N-terminal domain show a primarily helical fold that is analogous to the PWI fold found in several other RNA-binding proteins. Many recently discovered RNA-binding proteins (RBPs) do not show architectural similarities with classical RBPs, and their modes of interaction with RNA were unclear. We developed and employed RBDmap as a method for the comprehensive determination of the RNA-interacting sites of RBPs, identifying more than a thousand such sites. These data yield unprecedented insight into RNA-protein.
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N/a Ensembl ENSG n/a UniProt Q8IYB3 n/a RefSeq (mRNA) NM_ NM_ NM_ n/a RefSeq (protein) NP_ NP_ NP_ NP_ NP_ NP_ NP_ NP_ NP_ NP_ NP_ NP_ NP_ NP_ NP_ Aliases: SRRM1, KD, POP, SRM, serine and. Here the authors provide an extension to their earlier RNA interactome capture protocol.
This Protocol Extension describes RBDmap—a method to identify the regions of RNA-binding proteins engaged Cited by: SRm, the SR-related nuclear matrix protein of kDa, is a member of the SR proteins, which consists of a PWI motif for RNA binding at the N-terminus and a long and phosphorylated RS domain at the C-terminus (Eldridge et al., ; Szymczyna et al., ; Bodenmiller et al., ; Zhai et al., ).Author: Chen Qiu, Yu Zhang, Yu-Jie Fan, Ting-Lin Pang, Yan Su, Shuai Zhan, Yong-Zhen Xu.
Introduction. RNA metabolism relies on the dynamic interplay of RNAs with RNA-binding proteins (RBPs) forming ribonucleoprotein complexes, which control RNA fate from synthesis to decay (Glisovic et al., ).Due to their central role in cell biology, it is unsurprising that mutations in RBPs underlie numerous hereditary diseases (Castello et al., a, Lukong et al., ).Cited by: The RNA binding domain of CRV-ZWE is contained within the first 65 aa of the aa protein.
This also differentiates CRV-ZWE from the poxvirus E3L orthologs that have a Z-DNA binding domain at the N-terminus and the dsRNA binding domain at the C-terminus of the protein [ 18 ]. Molecular Cell Resource Comprehensive Identiﬁcation of RNA-Binding Domains in Human Cells Alfredo Castello,1,2,5 Bernd Fischer,1,3,5 Christian K.
Frese,1 Rastislav Horos,1 Anne-Marie Alleaume,1 Sophia Foehr,1 Tomaz Curk, 1,4 Jeroen Krijgsveld, 3 and Matthias W. Hentze1,* 1European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, Heidelberg, Germany. SBP2 is a novel protein of amino acids that contains a putative RNA binding domain similar to that found in the yeast SUP1 omnipotent suppressor of translation termination (Koonin et al., ).
We also report the first definitive incorporation of Sec into a selenoprotein translated in reticulocyte lysates. Little is known about how ADARs interact with their specific substrates and how the RNA binding domains and the catalytic domain work together during the editing reaction.
In contrast to the C-to-U RNA editing machinery that employs a primary sequence motif close to the editing site as critical determinant for substrate recognition (Niswender.
Gross T, Richert K, Mierke C, Lützelberger M, Käufer NF. Identification and characterization of srp1, a gene of fission yeast encoding a RNA binding domain and a RS domain typical of SR splicing factors. Nucleic Acids Res. Jan 15; 26 (2)– [PMC free article] Gui JF, Lane WS, Fu XD.
By yeast 2-hybrid, coimmunoprecipitation, and Western blot analyses, Loyer et al. () showed that the N terminus of the p isoform of PITSLRE (see CDC2L1; ), but not other isoforms, interacts with the N-terminal RNA-binding domain of fluorescence analysis demonstrated the expression of both proteins in large nuclear speckles.
We analyzed proteins containing nonclassical RNA‐binding domains and without annotated RNA‐binding domains with catRAPID signature and three other algorithms.
27, 68, 83, The performances are measured using a. accuracy, b. sensitivity, c. specificity, and d. precision. Feng GS, Chong K, Kumar A, Williams BR. Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase.
Proc Natl Acad Sci U S A. ; 89 (12)– [PMC free article]. We also discuss the identification of RNA targets Many RBPs have one or more copies of the same RNA binding domain while others have two or more distinct domains.
and Dreyfuss, G. Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm. Mol. Cell 6, – Kramer, K. et al. Photo-cross-linking and high-resolution mass spectrometry for assignment of RNA-binding sites in RNA-binding proteins.
Nat. Meth – (). The RNA-binding domain (fragment d) bound with a K′ a of ×10 7 M −1, an affinity of the order observed with certain ribosomal proteins. 27 Previously, free 35 S-labeled canine SRP72 that had been translated in reticulocyte lysates was unable to bind to SRP RNA, possibly due to a multitude of competing lysate factors.
RNA-binding proteins (RBPs) have essential roles in determining the fate of RNA from synthesis to decay and have been studied on a protein-by-protein basis, or.
Fernandez-Chamorro, J. et al. Identification of novel non-canonical RNA-binding sites in Gemin5 involved in internal initiation of translation. Nucleic Acids Res. 42, – (). The C. elegans genome encodes many RNA-binding proteins (RBPs) with diverse functions in development, indicative of extensive layers of post-transcriptional control of RNA metabolism.
A number of C. elegans RBPs have been identified by forward or reverse genetics. They tend to display tissue-specific mutant phenotypes, which underscore their functional importance. Competition assays showed that in both cases the order of affinity is dsRNA>VA RNA>tRNA, but the isolated motif bound much less tightly than the entire domain.
Measurement of the dissociation constants for dsRNA by quantitative gel mobility shift analysis gave apparent K d values of 4 x 10 −9 M and x 10 −7 M for p20 and p10, respectively. The Zebrafish Book. A Guide for the Laboratory Use of Zebrafish (Danio rerio).
Vacun G: Zebrafish as a model organism for the identification and characterization of drugs and genes affecting p53 signaling. Curr Biol (). Aravind L, Koonin EV () Novel predicted RNA-binding domains associated with the translation machinery.
J Mol Evol PubMed Google Scholar Aravind L, Koonin EV () THUMP -a predicted RNA-binding domain shared by 4-thiouridine, pseudouridine synthases and RNA methylases.The tonoplast monosaccharide transporter (TMT) family comprises three isoforms in Arabidopsis thaliana, and TMT–green fluorescent protein fusion proteins are targeted to the vacuolar membrane.
TMT promoter–β-glucuronidase plants revealed that the TONOPLAST MONOSACCHARIDE TRANSPORTER1 (TMT1) and TMT2 genes exhibit a tissue- and cell type–specific expression .Part of pre- and post-splicing multiprotein mRNP complexes.
Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during.