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  • 1
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    Reply to Hudgens et al.: Bald eagles, no-analog ecological scenarios, and conservation strategies on the Channel Islands [Letters (Online Only)] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-02-23
    Description: Hudgens et al. (1) raise two issues with our interpretation of past bald eagle diets on the Channel Islands (CI). First, they provide an alternative explanation for the terrestrial isotopic signatures of Pleistocene bald eagles from the CI, suggesting that they regularly fed on pygmy mammoth carrion (1). Although this explanation is plausible, it is not more parsimonious than the one that we provided (2). Movement data of reintroduced bald eagles show evidence of dispersal from the CI to the mainland, and in some cases, individuals return to the islands after using inland habitats across western North America (3). Such...
    Keywords: Letters
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 2
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    A spliceosomal recycling factor that reanneals U4 and U6 small nuclear ribonucleoprotein particles (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-28
    Description: The spliceosome removes introns from pre-messenger RNAs by a mechanism that entails extensive remodeling of RNA structure. The most conspicuous rearrangement involves disruption of 24 base pairs between U4 and U6 small nuclear RNAs (snRNAs). Here, the yeast RNA binding protein Prp24 is shown to reanneal these snRNAs. When Prp24 is absent, unpaired U4 and U6 small nuclear ribonucleoprotein particles (snRNPs) accumulate; with time, splicing becomes inhibited. Addition of purified Prp24 protein regenerates duplex U4/U6 snRNPs for new rounds of splicing. The reannealing reaction catalyzed by Prp24 proceeds more efficiently with snRNPs than with deproteinized snRNAs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raghunathan, P L -- Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 6;279(5352):857-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, San Francisco, School of Medicine, Department of Biochemistry and Biophysics, San Francisco, CA 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9452384" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Base Composition ; Fungal Proteins/*metabolism ; Models, Genetic ; *RNA Splicing ; RNA, Fungal/metabolism ; RNA, Small Nuclear/metabolism ; RNA-Binding Proteins/*metabolism ; Ribonucleoprotein, U4-U6 Small Nuclear/*metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; Spliceosomes/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Messenger RNA splicing in yeast: clues to why the spliceosome is a ribonucleoprotein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: The removal of introns from eukaryotic messenger RNA precursors shares mechanistic characteristics with the self-splicing of certain introns, prompting speculation that the catalytic reactions of nuclear pre-messenger RNA splicing are fundamentally RNA-based. The participation of five small nuclear RNAs (snRNAs) in splicing is now well documented. Genetic analysis in yeast has revealed the requirement, in addition, for several dozen proteins. Some of these are tightly bound to snRNAs to form small nuclear ribonucleoproteins (snRNPs); such proteins may promote interactions between snRNAs or between an snRNA and the intron. Other, non-snRNP proteins appear to associate transiently with the spliceosome. Some of these factors, which include RNA-dependent adenosine triphosphatases, may promote the accurate recognition of introns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):157-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1853200" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/physiology ; Base Sequence ; Fungal Proteins/genetics ; Molecular Sequence Data ; *RNA Splicing ; RNA, Fungal/*genetics ; RNA, Messenger/*genetics ; RNA, Small Nuclear/genetics ; Ribonucleoproteins/*physiology ; Saccharomyces cerevisiae/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Evolution of yeast noncoding RNAs reveals an alternative mechanism for widespread intron loss (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-11-06
    Description: The evolutionary forces responsible for intron loss are unresolved. Whereas research has focused on protein-coding genes, here we analyze noncoding small nucleolar RNA (snoRNA) genes in which introns, rather than exons, are typically the functional elements. Within the yeast lineage exemplified by the human pathogen Candida albicans, we find--through deep RNA sequencing and genome-wide annotation of splice junctions--extreme compaction and loss of associated exons, but retention of snoRNAs within introns. In the Saccharomyces yeast lineage, however, we find it is the introns that have been lost through widespread degeneration of splicing signals. This intron loss, perhaps facilitated by innovations in snoRNA processing, is distinct from that observed in protein-coding genes with respect to both mechanism and evolutionary timing.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3496775/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3496775/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mitrovich, Quinn M -- Tuch, Brian B -- De La Vega, Francisco M -- Guthrie, Christine -- Johnson, Alexander D -- GM021119/GM/NIGMS NIH HHS/ -- GM37049/GM/NIGMS NIH HHS/ -- R01 GM037049/GM/NIGMS NIH HHS/ -- R01 GM037049-26/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2010 Nov 5;330(6005):838-41. doi: 10.1126/science.1194554.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143-2200, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21051641" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Candida albicans/*genetics ; *Evolution, Molecular ; Exons ; Genome, Fungal ; *Introns ; Molecular Sequence Annotation ; RNA Splice Sites/genetics ; RNA Splicing ; RNA, Fungal/*genetics ; RNA, Small Nucleolar/*genetics ; Saccharomyces cerevisiae/*genetics ; Sequence Analysis, RNA ; Yeasts/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Molecular biology. Accurate RNA siting and splicing gets help from a DEK-hand (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kress, Tracy L -- Guthrie, Christine -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1886-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809518" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromatin Assembly and Disassembly ; Chromosomal Proteins, Non-Histone/*metabolism ; Dimerization ; Dinucleoside Phosphates/metabolism ; *Introns ; Models, Genetic ; Nuclear Proteins/metabolism ; Oncogene Proteins/*metabolism ; Phosphorylation ; RNA Precursors/*metabolism ; *RNA Splicing ; RNA, Messenger/metabolism ; Recombinant Proteins/metabolism ; Ribonucleoprotein, U2 Small Nuclear/metabolism ; Ribonucleoproteins/metabolism ; Spliceosomes/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Mutations in U6 snRNA that alter splice site specificity: implications for the active site (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-24
    Description: What determines the precise sites of cleavage in the two transesterification reactions of messenger RNA (mRNA) splicing is a major unsolved question. Mutation of the invariant G (guanosine) at position 5 of 5' splice sites in Saccharomyces cerevisiae introns activates cleavage at nearby aberrant sites. A genetic approach was used to test the hypothesis that a base-pairing interaction between the 5' splice site and the invariant ACAGAG sequence of U6 is a determinant of 5' splice site choice. Mutations in U6 or the intron (or both) that were predicted to stabilize the interaction suppressed aberrant cleavage and increased normal cleavage. In addition, a mutation in the ACAGAG sequence suppressed mutations of the 3' splice site dinucleotide. These data can fit a model for the spliceosomal active site comprised of a set of RNA-RNA interactions between the intron, U2 and U6.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lesser, C F -- Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):1982-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Scientist Training Program, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266093" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites/genetics ; Genes, Reporter ; Introns/genetics ; Models, Genetic ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Conformation ; RNA Splicing/*genetics ; RNA, Small Nuclear/*genetics ; Saccharomyces cerevisiae/genetics ; Suppression, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Essential yeast protein with unexpected similarity to subunits of mammalian cleavage and polyadenylation specificity factor (CPSF) (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-29
    Description: The 3' ends of most eukaryotic messenger RNAs are generated by internal cleavage and polyadenylation. In mammals, there is a strict dependence of both reactions on the sequence AAUAAA, which occurs upstream of polyadenylation [poly(A)] sites and which is recognized by CPSF. In contrast, cis-acting signals for yeast 3'-end generation are highly divergent from those of mammals, suggesting that trans-acting factors other than poly(A) polymerase would not be conserved. The essential yeast protein Brr5/Ysh1 shows sequence similarity to subunits of mammalian CPSF and is required for 3'-end processing in vivo and in vitro. These results demonstrate a structural and functional conservation of the yeast and mammalian 3'-end processing machineries despite a lack of conservation of the cis sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chanfreau, G -- Noble, S M -- Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1511-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, UCSF School of Medicine, San Francisco, CA 94143-0448. guthrie@cgl.ucsf.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929408" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; *Conserved Sequence ; Crystallography, X-Ray ; Fungal Proteins/*chemistry/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Poly A/metabolism ; RNA Precursors/metabolism ; *RNA Processing, Post-Transcriptional ; RNA, Fungal/metabolism ; RNA, Messenger/metabolism ; RNA-Binding Proteins/*chemistry/genetics/metabolism ; Saccharomyces cerevisiae/*chemistry/genetics ; mRNA Cleavage and Polyadenylation Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    A subset of yeast snRNA's contains functional binding sites for the highly conserved Sm antigen (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-01-16
    Description: Autoimmune sera of the Sm specificity react with the major class of small nuclear RNA (snRNA)-containing ribonucleoprotein particles (snRNP's) from organisms as evolutionarily divergent as insects and dinoflagellates but have been reported not to recognize snRNP's from yeast. The Sm antigen is thought to bind to a conserved snRNA motif that includes the sequence A(U3-6)G. The hypothesis was tested that yeast also contains functional analogues of Sm snRNA's, but that the Sm binding site in the RNA is more strictly conserved than the Sm antigenic determinant. After microinjection of labeled yeast snRNA's into Xenopus eggs or oocytes, two snRNA's from Saccharomyces cerevisiae become strongly immunoprecipitable with human auto-antibodies known as anti-Sm. These each contain the sequence A(U5-6)G, are essential for viability, and are constituents of the spliceosome. At least six other yeast snRNA's do not become immunoprecipitable and lack this sequence; these non-Sm snRNA's are all dispensable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riedel, N -- Wolin, S -- Guthrie, C -- GM 21119/GM/NIGMS NIH HHS/ -- GM 26875/GM/NIGMS NIH HHS/ -- GM 31286/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 16;235(4786):328-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2948278" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoantigens/*metabolism ; Binding Sites ; Protein Binding ; RNA, Small Nuclear/*metabolism ; Ribonucleoproteins/*metabolism ; Ribonucleoproteins, Small Nuclear ; Saccharomyces cerevisiae/*genetics/immunology ; Xenopus laevis ; snRNP Core Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Saccharomyces cerevisiae has a U1-like small nuclear RNA with unexpected properties (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-09-18
    Description: Previous experiments indicated that only a small subset of the approximately equal to 24 small nuclear RNAs (snRNAs) in Saccharomyces cerevisiae have binding sites for the Sm antigen, a hallmark of metazoan small nuclear ribonucleoproteins (snRNPs) involved in pre-messenger RNA splicing. Antibodies from human serum to Sm proteins were used to show that four snRNAs (snR7, snR14, snR19, and snR20) can be immunoprecipitated from yeast extracts. Three of these four, snR7, snR14, and snR20, have been shown to be analogs of mammalian U5, U4, and U2, respectively. Several regions of significant homology to U1 (164 nucleotides) have now been found in cloned and sequenced snR19 (568 nucleotides). These include ten out of ten matches to the 5' end of U1, the site known to interact with the 5' splice site of mammalian introns. Surprisingly, the precise conservation of this sequence precludes perfect complementarity between snR19 and the invariant yeast 5' junction (GTATGT), which differs from the mammalian consensus at the fourth position (GTPuAGT).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siliciano, P G -- Jones, M H -- Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Sep 18;237(4821):1484-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3306922" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies ; Autoantigens/metabolism ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Humans ; Nucleic Acid Conformation ; RNA, Fungal/analysis ; RNA, Small Nuclear/*analysis ; *Ribonucleoproteins, Small Nuclear ; Saccharomyces cerevisiae/*genetics ; snRNP Core Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Conservation in budding yeast of a kinase specific for SR splicing factors (1999)
    National Academy of Sciences
    Details
    Publication Date: 1999-05-11
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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