Controls on the Biosynthesis of Superoxide Dismutases in E. coli: An Inactive Precursor
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Kamal Shukla', 'PO_EMAI': None, 'PO_PHON': None}
Escherichia coli can produce two types of superoxide                            dismutases.  One of these, the iron enzyme is found in both                     aerobic and anaerobic cultures; while the second, a manganese                   enzyme, is ordinarily present only in aerobic cultures and                      can be strongly induced by hyperoxia, or by viologens and                       quinones which mediate intracellular production of O2-.  The                    manner in which the cell controls the biosynthesis of the                       manganese enzyme has been under study but is not yet                            understood.  This lab has reported that addition of an                          electron sink, such as paraquat plus nitrate, to an anaerobic                   culture causes production of the manganese enzyme in a form                     which is not active but which can be activated by addition of                   Mn(II) under mildly denaturing conditions; followed by                          removal of the denaturing stress.  This is referred to as the                   pro-enzyme.  It has also been shown that anaerobic cells                        contain another protein which is recognized by an antibody                      specific for the manganese enzyme, but which cannot be                          activated as can the pro-enzyme.  This protein is referred to                   this as the prepro-enzyme.  Experiments are being conducted                     to isolate, characterize and study the interconversions of                      these forms of the manganese-containing superoxide dismutase                    of E. coli.%%%                                                                                                                                                  Superoxide dismutases (SODs) are enzymes that provide                           defenses against the toxicity of molecular oxygen in living                     cells.  It also protects against other stresses, e.g., ultra-                   violet radiation and sulfur dioxide exposure.  How these                        enzymes are made is incompletely understood but important.                      The biosynthesis is probably regulated by environmental                         factors.  This project will elucidate the pathway of enzyme                     synthesis and activation.***//
{'FirstName': 'Irwin', 'LastName': 'Fridovich', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Irwin Fridovich', 'EmailAddress': '9196848885', 'NSF_ID': '000180919', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Duke University', 'CityName': 'DURHAM', 'ZipCode': '277054640', 'PhoneNumber': '9196843030', 'StreetAddress': '2200 W MAIN ST', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'North Carolina', 'StateCode': 'NC', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'NC04', 'ORG_UEI_NUM': 'TP7EK8DZV6N5', 'ORG_LGL_BUS_NAME': 'DUKE UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
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