Experts and Doctors on rna precursors in Chapel Hill, North Carolina, United States


Locale: Chapel Hill, North Carolina, United States
Topic: rna precursors

Top Publications

  1. Lane K, Yu Y, Lackey P, Chen X, Marzluff W, Cook J. Cell cycle-regulated protein abundance changes in synchronously proliferating HeLa cells include regulation of pre-mRNA splicing proteins. PLoS ONE. 2013;8:e58456 pubmed publisher
    ..Comparison of this dataset to several other proteomic datasets sheds light on global mechanisms of cell cycle phase transitions and underscores the importance of both phosphorylation and ubiquitination in cell cycle changes. ..
  2. Lacerra G, Sierakowska H, Carestia C, Fucharoen S, Summerton J, Weller D, et al. Restoration of hemoglobin A synthesis in erythroid cells from peripheral blood of thalassemic patients. Proc Natl Acad Sci U S A. 2000;97:9591-6 pubmed
    ..Thus, expression of defective beta-globin genes was repaired and significant level of Hb A was restored in a cell population that would be targeted in clinical applications of this approach. ..
  3. Wang Y, Cheong C, Hall T, Wang Z. Engineering splicing factors with designed specificities. Nat Methods. 2009;6:825-30 pubmed publisher
    ..Our approach permitted the creation of artificial factors to target virtually any pre-mRNA, providing a strategy to study splicing regulation and to manipulate disease-associated splicing events. ..
  4. Svasti S, Suwanmanee T, Fucharoen S, Moulton H, Nelson M, Maeda N, et al. RNA repair restores hemoglobin expression in IVS2-654 thalassemic mice. Proc Natl Acad Sci U S A. 2009;106:1205-10 pubmed publisher
    ..Repaired beta-globin mRNA restored significant amounts of hemoglobin in the peripheral blood of the IVS2-654 mouse, improving the number and quality of erythroid cells. ..
  5. Yang X, Sabath I, Debski J, Kaus Drobek M, Dadlez M, Marzluff W, et al. A complex containing the CPSF73 endonuclease and other polyadenylation factors associates with U7 snRNP and is recruited to histone pre-mRNA for 3'-end processing. Mol Cell Biol. 2013;33:28-37 pubmed publisher
  6. Yang X, Sullivan K, Marzluff W, Dominski Z. Studies of the 5' exonuclease and endonuclease activities of CPSF-73 in histone pre-mRNA processing. Mol Cell Biol. 2009;29:31-42 pubmed publisher
    ..RNA interference experiments with HeLa cells indicate that degradation of the DCP does not depend on the Xrn2 5' exonuclease, suggesting that CPSF-73 degrades the DCP both in vitro and in vivo. ..
  7. Aik W, Lin M, Tan D, Tripathy A, Marzluff W, Dominski Z, et al. The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing. PLoS ONE. 2017;12:e0186034 pubmed publisher
    ..Using solution light scattering, we characterized the stoichiometry of the FLASH NTD-Lsm11 NTD complex and found that it is a 2:1 heterotrimer, which is supported by observations from analytical ultracentrifugation and crosslinking. ..
  8. Westdorp K, Sand A, Moorman N, Terhune S. Cytomegalovirus Late Protein pUL31 Alters Pre-rRNA Expression and Nuclear Organization during Infection. J Virol. 2017;91: pubmed publisher
    ..Understanding these processes will help define approaches to stimulate cellular intrinsic stress responses that are capable of inhibiting CMV infection. ..
  9. Yang X, Xu B, Sabath I, Kunduru L, Burch B, Marzluff W, et al. FLASH is required for the endonucleolytic cleavage of histone pre-mRNAs but is dispensable for the 5' exonucleolytic degradation of the downstream cleavage product. Mol Cell Biol. 2011;31:1492-502 pubmed publisher
    ..These results suggest that CPSF-73, the catalytic component in both reactions, can be recruited to histone pre-mRNA largely in a manner independent of FLASH, possibly by a separate domain in Lsm11. ..

More Information


  1. Wan J, Sazani P, Kole R. Modification of HER2 pre-mRNA alternative splicing and its effects on breast cancer cells. Int J Cancer. 2009;124:772-7 pubmed publisher
    ..Both SSO111 and Delta15HER2 may be potential candidates for the development of novel HER2-targeted cancer therapeutics. ..
  2. Marzluff W. U2 snRNP: not just for poly(A) mRNAs. Mol Cell. 2007;28:353-4 pubmed
    ..Friend et al. (2007) now report that the U2 snRNP, required for pre-mRNA splicing, is also required for histone mRNA 3' end formation. ..
  3. Murray M, Turnage M, Williamson K, Steinhauer W, Searles L. The Drosophila suppressor of sable protein binds to RNA and associates with a subset of polytene chromosome bands. Mol Cell Biol. 1997;17:2291-300 pubmed
    ..Considering these and previous results, we propose two models to explain how su(s) mutations affect nuclear pre-mRNA processing. ..
  4. Kuan Y, Brewer Jensen P, Searles L. Suppressor of sable, a putative RNA-processing protein, functions at the level of transcription. Mol Cell Biol. 2004;24:3734-46 pubmed
    ..Together, these results reveal a link between Su(s), transcription, and pre-mRNA processing. ..
  5. SORENSON M, Jha D, Ucles S, Flood D, Strahl B, Stevens S, et al. Histone H3K36 methylation regulates pre-mRNA splicing in Saccharomyces cerevisiae. RNA Biol. 2016;13:412-26 pubmed publisher
    ..Additionally, we found that deletion of SET2 reduces the association of the U2 and U5 snRNPs with chromatin. Thus, our study provides the first evidence that H3K36 methylation plays a role in co-transcriptional RNA splicing in yeast. ..
  6. Matera A, Wang Z. A day in the life of the spliceosome. Nat Rev Mol Cell Biol. 2014;15:108-21 pubmed publisher
    ..This assembly process can also affect the regulation of alternative splicing and has implications for human disease. ..
  7. Wang Y, Ma M, Xiao X, Wang Z. Intronic splicing enhancers, cognate splicing factors and context-dependent regulation rules. Nat Struct Mol Biol. 2012;19:1044-52 pubmed publisher
    ..We provide a comprehensive picture of general ISE activities and suggest new models of how single elements can function oppositely, depending on locations and binding factors. ..
  8. Salzler H, Davidson J, Montgomery N, Duronio R. Loss of the histone pre-mRNA processing factor stem-loop binding protein in Drosophila causes genomic instability and impaired cellular proliferation. PLoS ONE. 2009;4:e8168 pubmed publisher
  9. Sullivan K, Steiniger M, Marzluff W. A core complex of CPSF73, CPSF100, and Symplekin may form two different cleavage factors for processing of poly(A) and histone mRNAs. Mol Cell. 2009;34:322-32 pubmed publisher
    ..These results suggest that a common core cleavage factor is required for processing of histone and polyadenylated pre-mRNAs. ..
  10. Dominski Z, Zheng L, Sanchez R, Marzluff W. Stem-loop binding protein facilitates 3'-end formation by stabilizing U7 snRNP binding to histone pre-mRNA. Mol Cell Biol. 1999;19:3561-70 pubmed
    ..One role of SLBP is to stabilize the interaction of the histone pre-mRNA with U7 snRNP. ..
  11. Dominski Z, Erkmann J, Greenland J, Marzluff W. Mutations in the RNA binding domain of stem-loop binding protein define separable requirements for RNA binding and for histone pre-mRNA processing. Mol Cell Biol. 2001;21:2008-17 pubmed
    ..It is likely that the RBD of SLBP interacts directly with both the stem-loop RNA and other processing factor(s), most likely the U7 snRNP, to facilitate histone pre-mRNA processing. ..
  12. Dominski Z, Yang X, Marzluff W. The polyadenylation factor CPSF-73 is involved in histone-pre-mRNA processing. Cell. 2005;123:37-48 pubmed
    ..These studies suggest that CPSF-73 is both the endonuclease and 5'-3' exonuclease in histone-pre-mRNA processing and reveal an evolutionary link between 3' end formation of histone mRNAs and polyadenylated mRNAs. ..
  13. Dominski Z, Erkmann J, Yang X, Sanchez R, Marzluff W. A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3'-end processing. Genes Dev. 2002;16:58-71 pubmed
    ..Antibodies to hZFP100 precipitate U7 snRNA, and expression of hZFP100 in Xenopus oocytes stimulates processing of histone pre-mRNA, showing that hZFP100 is a component of the processing machinery. ..
  14. Fridell R, Pret A, Searles L. A retrotransposon 412 insertion within an exon of the Drosophila melanogaster vermilion gene is spliced from the precursor RNA. Genes Dev. 1990;4:559-66 pubmed
    ..Four different 5' donor sites are alternatively spliced to a single 3' acceptor site. The implications of this finding are discussed in relation to possible functions of the su(s)+ gene product. ..
  15. Gonsalvez G, Rajendra T, Wen Y, Praveen K, Matera A. Sm proteins specify germ cell fate by facilitating oskar mRNA localization. Development. 2010;137:2341-51 pubmed publisher
    ..We conclude that Sm proteins function to establish the germline in Drosophila, at least in part by mediating oskar mRNA localization. ..
  16. Godfrey A, White A, Tatomer D, Marzluff W, Duronio R. The Drosophila U7 snRNP proteins Lsm10 and Lsm11 are required for histone pre-mRNA processing and play an essential role in development. RNA. 2009;15:1661-72 pubmed publisher
  17. Wang Z, Burge C. Splicing regulation: from a parts list of regulatory elements to an integrated splicing code. RNA. 2008;14:802-13 pubmed publisher
    ..Here, we summarize the current state of knowledge of splicing cis-regulatory elements and their context-dependent effects on splicing, emphasizing recent global/genome-wide studies and open questions. ..
  18. Wagner E, Burch B, Godfrey A, Salzler H, Duronio R, Marzluff W. A genome-wide RNA interference screen reveals that variant histones are necessary for replication-dependent histone pre-mRNA processing. Mol Cell. 2007;28:692-9 pubmed
  19. Wagner E, Marzluff W. ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA processing, is required for entry into S phase. Mol Cell Biol. 2006;26:6702-12 pubmed
  20. Dominski Z, Yang X, Purdy M, Marzluff W. Differences and similarities between Drosophila and mammalian 3' end processing of histone pre-mRNAs. RNA. 2005;11:1835-47 pubmed
  21. Lanzotti D, Kupsco J, Yang X, Dominski Z, Marzluff W, Duronio R. Drosophila stem-loop binding protein intracellular localization is mediated by phosphorylation and is required for cell cycle-regulated histone mRNA expression. Mol Biol Cell. 2004;15:1112-23 pubmed
    ..The T230A protein is concentrated in the cytoplasm, suggesting that it is defective in nuclear targeting, and accounting for its failure to function in histone pre-mRNA processing in vivo. ..
  22. Burch B, Godfrey A, Gasdaska P, Salzler H, Duronio R, Marzluff W, et al. Interaction between FLASH and Lsm11 is essential for histone pre-mRNA processing in vivo in Drosophila. RNA. 2011;17:1132-47 pubmed publisher
    ..Together, these studies demonstrate that direct interaction between dFLASH and dLsm11 is essential for histone pre-mRNA processing in vivo and for proper development and viability in flies. ..
  23. White A, Burch B, Yang X, Gasdaska P, Dominski Z, Marzluff W, et al. Drosophila histone locus bodies form by hierarchical recruitment of components. J Cell Biol. 2011;193:677-94 pubmed publisher
  24. Whitfield M, Kaygun H, Erkmann J, Townley Tilson W, Dominski Z, Marzluff W. SLBP is associated with histone mRNA on polyribosomes as a component of the histone mRNP. Nucleic Acids Res. 2004;32:4833-42 pubmed
    ..SLBP remains active both in RNA binding and histone pre-mRNA processing when DNA replication is inhibited. ..
  25. Dominski Z. Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism. Crit Rev Biochem Mol Biol. 2007;42:67-93 pubmed
    ..This article reviews the cellular roles of nucleases of the metallo-beta-lactamase family and the recent advances in studying these proteins. ..
  26. White A, Leslie M, Calvi B, Marzluff W, Duronio R. Developmental and cell cycle regulation of the Drosophila histone locus body. Mol Biol Cell. 2007;18:2491-502 pubmed
    ..HLB foci are present in histone deletion embryos, although the MPM-2 foci are smaller, and some Lsm11 foci are not associated with MPM-2 foci, suggesting that the histone locus is important for HLB integrity. ..
  27. Yang X, Torres M, Marzluff W, Dominski Z. Three proteins of the U7-specific Sm ring function as the molecular ruler to determine the site of 3'-end processing in mammalian histone pre-mRNA. Mol Cell Biol. 2009;29:4045-56 pubmed publisher
    ..These proteins likely rigidify the substrate and function as the molecular ruler in determining the site of cleavage. ..
  28. Yang X, Burch B, Yan Y, Marzluff W, Dominski Z. FLASH, a proapoptotic protein involved in activation of caspase-8, is essential for 3' end processing of histone pre-mRNAs. Mol Cell. 2009;36:267-78 pubmed publisher
    ..These results demonstrate that FLASH is an essential factor required for 3' end maturation of histone mRNAs in both vertebrates and invertebrates and suggest a potential link between this process and apoptosis. ..
  29. Underwood M, Fried H. Characterization of nuclear localizing sequences derived from yeast ribosomal protein L29. EMBO J. 1990;9:91-9 pubmed
    ..These results were as expected if the two short peptide sequences functioned in nuclear localization and/or assembly of yeast ribosomal protein L29. ..
  30. Newman M, Hammond S. Emerging paradigms of regulated microRNA processing. Genes Dev. 2010;24:1086-92 pubmed publisher
    ..The second paradigm is specific to miRNA families, and requires interaction between RNA-binding proteins and cis-regulatory sequences within miRNA precursor loops. ..
  31. Dominski Z, Marzluff W. Formation of the 3' end of histone mRNA. Gene. 1999;239:1-14 pubmed
    ..One of the major regulatory events in the cell cycle is regulation of histone pre-mRNA processing, which is at least partially mediated by cell-cycle regulation of the levels of the SLBP protein. ..
  32. Godfrey A, Kupsco J, Burch B, Zimmerman R, Dominski Z, Marzluff W, et al. U7 snRNA mutations in Drosophila block histone pre-mRNA processing and disrupt oogenesis. RNA. 2006;12:396-409 pubmed
    ..These data suggest that SLBP and U7 snRNP cooperate in the production of histone mRNA in vivo, and that disruption of histone pre-mRNA processing is detrimental to development. ..