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Strontium Isotope Ages of the Marine Merced Formation, near San Francisco, California
- B. Lynn Ingram, James C. Ingle
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- Journal:
- Quaternary Research / Volume 50 / Issue 2 / September 1998
- Published online by Cambridge University Press:
- 20 January 2017, pp. 194-199
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The strontium isotopic compositions of foraminifers ( Elphidiella hannaiwere determined to refine the age of coastal sediments of the Merced Formation and to evaluate the relation between transgressive–regressive cycles and Pleistocene glacio-eustatic sea-level fluctuations. Relatively good age resolution (± 0.1 myr) is possible in the upper part of the section. The Sr isotope ages provide strong supporting evidence for the fission track ages of an ash layer at the top of the formation (0.45 myr), as well as recent age estimates for the mammoth fossil of ∼0.45 myr. Sr isotope ages in the upper part of the section also confirm that marine/nonmarine cyclic sedimentation in the Merced Formation is controlled by glacial–interglacial cycles. Good age resolution for the lower part of the section is not possible, due to little variation of the87Sr/86Sr ratio in global sea water between 2.4 and 4.3 myr. The age of the base of the formation is constrained only between 2.4 and 4.8 myr. Sediment accumulation rates in the upper portion of the Merced Formation (between 0 and 720 m) are significantly higher than those calculated for the basal portion (between 720 and 1670 m). The change in accumulation rate may be due to increased continental weathering rates and/or increased tectonic subsidence beginning about 0.8 myr ago.
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- By Rose Teteki Abbey, K. C. Abraham, David Tuesday Adamo, LeRoy H. Aden, Efrain Agosto, Victor Aguilan, Gillian T. W. Ahlgren, Charanjit Kaur AjitSingh, Dorothy B E A Akoto, Giuseppe Alberigo, Daniel E. Albrecht, Ruth Albrecht, Daniel O. Aleshire, Urs Altermatt, Anand Amaladass, Michael Amaladoss, James N. Amanze, Lesley G. Anderson, Thomas C. Anderson, Victor Anderson, Hope S. Antone, María Pilar Aquino, Paula Arai, Victorio Araya Guillén, S. Wesley Ariarajah, Ellen T. Armour, Brett Gregory Armstrong, Atsuhiro Asano, Naim Stifan Ateek, Mahmoud Ayoub, John Alembillah Azumah, Mercedes L. García Bachmann, Irena Backus, J. Wayne Baker, Mieke Bal, Lewis V. Baldwin, William Barbieri, António Barbosa da Silva, David Basinger, Bolaji Olukemi Bateye, Oswald Bayer, Daniel H. Bays, Rosalie Beck, Nancy Elizabeth Bedford, Guy-Thomas Bedouelle, Chorbishop Seely Beggiani, Wolfgang Behringer, Christopher M. Bellitto, Byard Bennett, Harold V. Bennett, Teresa Berger, Miguel A. 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- 05 August 2012
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- 20 September 2010, pp xi-xliv
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Splicing and transcription-associated proteins PSF and p54nrb/NonO bind to the RNA polymerase II CTD
- ANDREW EMILI, MICHAEL SHALES, SUSAN McCRACKEN, WEIJUN XIE, PHILIP W. TUCKER, RYUJI KOBAYASHI, BENJAMIN J. BLENCOWE, C. JAMES INGLES
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The carboxyl-terminal domain (CTD) of the largest subunit of eukaryotic RNA polymerase II (pol II) plays an important role in promoting steps of pre-mRNA processing. To identify proteins in human cells that bind to the CTD and that could mediate its functions in pre-mRNA processing, we used the mouse CTD expressed in bacterial cells in affinity chromatography experiments. Two proteins present in HeLa cell extract, the splicing and transcription-associated factors, PSF and p54nrb/NonO, bound specifically and could be purified to virtual homogeneity by chromatography on immobilized CTD matrices. Both hypo- and hyperphosphorylated CTD matrices bound these proteins with similar selectivity. PSF and p54nrb/NonO also copurified with a holoenzyme form of pol II containing hypophosphorylated CTD and could be coimmunoprecipitated with antibodies specific for this and the hyperphosphorylated form of pol II. That PSF and p54nrb/NonO promoted the binding of RNA to immobilized CTD matrices suggested these proteins can interact with the CTD and RNA simultaneously. PSF and p54nrb/NonO may therefore provide a direct physical link between the pol II CTD and pre-mRNA processing components, at both the initiation and elongation phases of transcription.