PEST Sequences as Signals for Rapid Proteolysis
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'M.  Paige', 'PO_EMAI': None, 'PO_PHON': None}
Rapidly degraded proteins contain sequences rich in proline (P),                glutamic acid (E), serine (S) and threonine (T), and it is                      proposed that these PEST regions confer metabolic instability                   upon proteins possessing them.  Although the evidence supporting                of the PEST hypothesis has increased substantially over the past                year, it is still mostly correlative.  This research tests the                  hypothesis directly, elucidates those features of PEST regions                  essential for rapid proteolysis and elucidates the mechanism(s)                 by which PEST proteins are degraded.  PEST-conjugated proteins                  will be radio-iodinated and their metabolic stabilities measured                by introducing them into cultured mammalian cells using RBC-                    mediated injection.  Alternatively PEST sequences will be cloned                onto the N terminus of dihydrofolate reductase, and injected into               mammalian culture cells.  By varying residues within the                        synthesized or cloned PEST sequences, essential features of the                 degradation signal should be discovered.  Using differentially                  labeled wild-type and PEST-deleted ornithine decarboxylase                      molecules it will be possible to distinguish PEST-specific                      proteolysis from indiscriminate cleavage.                                                                                                                       Most proteins are studied from the point of view of their                       synthesis.  Yet the living cell makes and degrades proteins in                  its normal functioning.  This study centers on an innovative                    hypothesis about how the cell chooses which proteins to degrade                 and when to do it.  This is an underexplored but important topic                in cellular biochemistry.
{'FirstName': 'Martin', 'LastName': 'Rechsteiner', 'PI_MID_INIT': 'C', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Martin C Rechsteiner', 'EmailAddress': None, 'NSF_ID': '000474483', 'StartDate': '09/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Utah', 'CityName': 'SALT LAKE CITY', 'ZipCode': '841129049', 'PhoneNumber': '8015816903', 'StreetAddress': '201 PRESIDENTS CIR', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Utah', 'StateCode': 'UT', 'CONGRESSDISTRICT': '01', 'CONGRESS_DISTRICT_ORG': 'UT01', 'ORG_UEI_NUM': 'LL8GLEVH6MG3', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF UTAH', 'ORG_PRNT_UEI_NUM': None}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8816560.xml'}