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The Recombinant Expression and Potential Applications of Bacterial Organophosphate

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The Recombinant Expression and Potential Applications of Bacterial Organophosphate View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Texas A&M Repository THE RECOMBINANT EXPRESSION AND POTENTIAL APPLICATIONS OF BACTERIAL ORGANOPHOSPHATE HYDROLASE IN Zea mays L. A Dissertation by TERRENCE SCOTT PINKERTON Submitted to the Office of Graduate Studies of Texas A&M University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY May 2004 Major Subject: Biochemistry THE RECOMBINANT EXPRESSION AND POTENTIAL APPLICATIONS OF BACTERIAL ORGANOPHOSPHATE HYDROLASE IN Zea mays L. A Dissertation by TERRENCE SCOTT PINKERTON Submitted to Texas A&M University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Approved as to style and content by: James R. Wild John A. Howard (Chair of Committee) (Member) J. Martin Scholtz William D. Park (Member) (Member) Stephen H. Safe Gregory D. Reinhart (Member) (Head of Department) May 2004 Major Subject: Biochemistry iii ABSTRACT The Recombinant Expression and Potential Applications of Bacterial Organophosphate Hydrolase in Zea mays L. (May 2004) Terrence Scott Pinkerton, B.S., University of Nebraska-Lincoln Chair of Advisory Committee: Dr. James R. Wild Organophosphate hydrolase (OPH, EC 3.1.8.1) is a bacterial enzyme with a broad spectrum of potential substrates that include organophosphorus pesticides, herbicides, and chemical warfare agents. OPH has been expressed successfully in bacterial, fungal, and insect cell culture systems; however, none of these systems produces amounts of enzyme suitable for applications outside of the research laboratory. Therefore, a transgenic Zea mays L. (maize) system was developed to express OPH as an alternate to the current OPH expression systems. The bacterial gene encoding the OPH protein was optimized for transcriptional and translational expression in maize. The optimized gene was inserted into the maize genome under the control of embryo specific, endosperm specific, and constitutive plant promoters. Select transformants were analyzed for the expression of OPH. Expression was observed in the seeds of plants transformed with each of the three constructs with the highest expression observed with the embryo specific and constitutive promoter constructs. The highest OPH expressing lines of transgenic maize had expression levels higher than those reported for the E. coli expression system. OPH was purified from transgenic maize seed and analyzed for post- translational modification and kinetic properties. OPH was observed to undergo a iv glycosylation event when expressed in maize that yielded at least two forms of OPH homogolous dimer. The glycosylated form of OPH bound tightly to the Concanavalin A sepharose and remained active after months of storage at room temperature. OPH activity was checked against a number of organophosphate herbicides. Enzymatic activity was observed against the herbicide Amiprophos-methyl and kinetic properties were measured. Enzymatic activity was also tested against the organophosphate Haloxon. Transgenic maize callus, leaf, and seed tissue could be screened for the presence of the optimized opd gene by enzymatic activity. Comparison of the growth of transgenic and control callus on media containing organophosphates showed that the transgenic callus was resistant to the herbicidal effects of haloxon. Transgenic plants expressing OPH were also resistant to the herbicide bensulide when compared to control plants. This indicates that OPH can be used as a screenable marker in plant systems and may be a potential scorable marker system as well. v ACKNOWLEDGMENTS I would like to express my appreciation to the following people and organizations for helping me to achieve my goals. First I would like to thank my committee for the time spent advising me on my graduate career. I would like to express my gratitude to Dr. Jim Wild for serving as my committee chair and Dr. John Howard for helping to direct my research. I would also like to thank Tony Reeves who provided the graphic for Figure 16 and Dr. Janet Grimsley who provided purified recombinant OPH from E. coli. I would like to express my appreciation to ProdiGeneâ for providing the funding and the physical workspace for me to attempt this project. I would like to thank the following current and former ProdiGeneâ employees for the assistance that they contributed: Dr. Joe Jilka, for helping with the initial design and construction of the optimized opd gene. Kathy Beifuss, without whom the final completion of the optimized gene and the expression vectors would not have been accomplished; Michele Bailey, who helped greatly with ideas for seed analysis and characterization of glycosylation; Mike Horn, Amanda Vinas, and Jeff Lane for helping with the transformation of OPH constructs and the generation of kill curve data; Karen Ruby for helping with experiments involving the use of OPH as a scorable marker; and Carol Drees and the greenhouse staff for assisting with the care of my transgenic plants and help in experimentation. vi I would like to thank my family for supporting and encouraging me in my endeavors. Finally I would like to thank my wife, Jennifer, for the years of support she has provided while I was trying to accomplish this goal. vii TABLE OF CONTENTS Page ABSTRACT............................................................................................................... iii ACKNOWLEDGMENTS.......................................................................................... v TABLE OF CONTENTS ........................................................................................... vii LIST OF FIGURES.................................................................................................... ix LIST OF TABLES...................................................................................................... xi CHAPTER I INTRODUCTION ................................................................................ 1 II OPTIMIZATION, CONSTRUCTION, AND EXPRESSION OF A BACTERIAL ORGANOPHOSPHATE HYDROLASE GENE IN Zea mays L........................................................................... 10 Introduction............................................................................. 10 Results .................................................................................... 13 Disscussion.............................................................................. 29 Materials and Methods............................................................ 33 III PURIFICATION AND CHARACTERIZATION OF ORGANOPHOSPHATE HYDROLASE EXPRESSED RECOMBINANTLY IN Zea mays L.................................................... 40 Introduction............................................................................. 40 Results .................................................................................... 44 Discussion............................................................................... 53 Materials and Methods............................................................ 57 IV ENZYMATIC DEGRADATION OF AN ORGANOPHOSPHATE HERBICIDE BY ORGANOPHOSPHATE HYDROLASE................... 61 Introduction............................................................................. 63 Results .................................................................................... 66 Discussion............................................................................... 71 Materials and Methods............................................................ 77 viii CHAPTER Page V ORGANOPHOSPHATE HYDROLASE AS A MARKER SYSTEM FOR TRANSGENIC MAIZE ............................................... 80 Introduction............................................................................. 80 Results .................................................................................... 83 Discussion............................................................................... 101 Materials and Methods............................................................ 105 VI CONCLUSIONS.................................................................................. 110 REFERENCES........................................................................................................... 119 APPENDIX A MAIZE HIGH CODON TABLE AND CHANGES TO THE NATIVE opd GENE...................................................... 128 APPENDIX B OPA AND OPB T1 SEED EXPRESSION DATA....................... 131 APPENDIX C OPH EXPRESSION IN T2 AND HIGHER SEED....................... 141 APPENDIX D SCORING OF TRANSGENIC CALLUS.................................... 155 VITA.......................................................................................................................... 159 ix LIST OF FIGURES FIGURE Page 1 Assembly of the Optimized opd Gene ............................................... 14 2 Optimized opd Gene Sequence......................................................... 15 3 Assembled Maize Transformation Vectors ........................................ 17 4 Paraoxonase Activity of Transgenic Callus......................................... 18 5 Increase of Enzymatic Activity in Seed Extract after Incubation with Transition Metal Salt.................................................................. 19 6 In Gel Hydrolysis of Coumaphos by OPA Seed Extract .................... 20 7 Temperature Effect on the Increase of Activity Detected in Seed Extract Incubated with 10mM CoCl2 ................................................ 22 8 Effect of Bicarbonate on the Incubation of Seed Extract
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