TY - SOUND TI - Metals in Biology AU - Hassan, H.M. DA - 1995/// PY - 1995/// ER - TY - JOUR TI - Binding of integration host factor (IHF) to the Escherichia coli sodA gene and its role in the regulation of a sodA-lacZ fusion gene AU - Presutti, David G. AU - Hassan, Hosni M. T2 - Molecular and General Genetics MGG DA - 1995/3// PY - 1995/3// DO - 10.1007/bf00294686 VL - 246 IS - 2 SP - 228-235 J2 - Molec. Gen. Genet. LA - en OP - SN - 0026-8925 1432-1874 UR - http://dx.doi.org/10.1007/bf00294686 DB - Crossref KW - ESCHERICHIA COLI KW - SUPEROXIDE DISMUTASE (SOD) KW - INTEGRATION HOST FACTOR (IHF) KW - MOBILITY-SHIFT ER - TY - JOUR TI - A geminivirus induces expression of a host DNA synthesis protein in terminally differentiated plant cells. AU - Nagar, S AU - Pedersen, T J AU - Carrick, K M AU - Hanley-Bowdoin, L AU - Robertson, D T2 - The Plant Cell AB - Geminiviruses are plant DNA viruses that replicate through DNA intermediates in plant nuclei. The viral components required for replication are known, but no host factors have yet been identified. We used immunolocalization to show that the replication proteins of the geminivirus tomato golden mosaic virus (TGMV) are located in nuclei of terminally differentiated cells that have left the cell cycle. In addition, TGMV infection resulted in a significant accumulation of the host DNA synthesis protein proliferating cell nuclear antigen (PCNA). PCNA, an accessory factor for DNA polymerase delta, was not present at detectable levels in healthy differentiated cells. The TGMV replication protein AL1 was sufficient to induce accumulation of PCNA in terminally differentiated cells of transgenic plants. Analysis of the mechanism(s) whereby AL1 induces the accumulation of host replication machinery in quiescent plant cells will provide a unique opportunity to study plant DNA synthesis. DA - 1995/6// PY - 1995/6// DO - 10.1105/tpc.7.6.705 VL - 7 IS - 6 SP - 705-719 J2 - Plant Cell LA - en OP - SN - 1040-4651 1532-298X UR - http://dx.doi.org/10.1105/tpc.7.6.705 DB - Crossref ER - TY - JOUR TI - FORMATION OF THE FERRITIN IRON MINERAL OCCURS IN PLASTIDS - AN X-RAY-ABSORPTION SPECTROSCOPY STUDY AU - WALDO, GS AU - WRIGHT, E AU - WHANG, ZH AU - BRIAT, JF AU - THEIL, EC AU - SAYERS, DE T2 - PLANT PHYSIOLOGY AB - Ferritin in plants is a nuclear-encoded, multisubunit protein found in plastids; an N-terminal transit peptide targets the protein to the plastid, but the site for formation of the ferritin Fe mineral is unknown. In biology, ferritin is required to concentrate Fe to levels needed by cells (approximately 10–7 M), far above the solubility of the free ion (10–18 M); the protein directs the reversible phase transition of the hydrated metal ion in solution to hydrated Fe-oxo mineral. Low phosphate characterizes the solid-phase Fe mineral in the center of ferritin of the cytosolic animal ferritin, but high phosphate is the hallmark of Fe mineral in prokaryotic ferritin and plant (pea [Pisum sativum L.] seed) ferritin. Earlier studies using x-ray absorption spectroscopy showed that high concentrations of phosphate present during ferritin mineralization in vitro altered the local structure of Fe in the ferritin mineral so that it mimicked the prokaryotic type, whether the protein was from animals or bacteria. The use of x-ray absorption spectroscopy to analyze the Fe environment in pea-seed ferritin now shows that the natural ferritin mineral in plants has an Fe-P interaction at 3.26A, similar to that of bacterial ferritin; phosphate also prevented formation of the longer Fe-Fe interactions at 3.5A found in animal ferritins or in pea-seed ferritin reconstituted without phosphate. Such results indicate that ferritin mineralization occurs in the plastid, where the phosphate content is higher; a corollary is the existence of a plastid Fe uptake system to allow the concentration of Fe in the ferritin mineral. DA - 1995/11// PY - 1995/11// DO - 10.1104/pp.109.3.797 VL - 109 IS - 3 SP - 797-802 SN - 1532-2548 ER - TY - JOUR TI - Localization of diacylglycerol acyltransferase to oil body associated endoplasmic reticulum AU - Settlage, S. B. AU - Wilson, R. F. AU - Kwanyuen, P. T2 - Plant Physiology and Biochemistry DA - 1995/// PY - 1995/// VL - 33 IS - 4 SP - 399 ER - TY - PAT TI - Displacement chromatography process AU - Pliura, D. H. AU - Wiffen, D. E. AU - Ashraf, S. AU - Magnin, A. A. C2 - 1995/// DA - 1995/// PY - 1995/// ER - TY - JOUR TI - Functional implications of the structure of the bacterial response regulator Spo0F AU - Feher, V. A. AU - Zapf, J. AU - Hoch, J. A. AU - Whiteley, J. M. AU - Cavanagh, J. AU - W., Dahlquist F. T2 - Journal of Cellular Biochemistry DA - 1995/// PY - 1995/// VL - Suppl. 21B SP - 25 ER - TY - JOUR TI - LIGNIN BIOSYNTHESIS AU - WHETTEN, R AU - SEDEROFF, R T2 - PLANT CELL DA - 1995/7// PY - 1995/7// DO - 10.2307/3870053 VL - 7 IS - 7 SP - 1001-1013 SN - 1532-298X ER -