Antitermination of Transcription by Phage Lambda's N        Mutational Analysis.
{'Code': '08070100', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Philip Harriman', 'PO_EMAI': None, 'PO_PHON': None}
The long range objective is to characterize the molecular                       interactions among Nus proteins of E. coli and N protein of                     bacteriophage lambda and a phage-coded nucleic acid recognition                 site, the effect of which is to modify transcription with respect               to its ability to pause and terminate.  The "antitermination"                   consequence of lambdoid phage infection takes effect subsequent                 to transcription initiation, and is thus distinct from regulation               of the initiation process. Now that the phage components for                    antitermination have been separated by DNA cloning, we are well                 positioned to investigate the molecular structure of those                      components and the means by which they interact, probably with                  the RNA transcript, to modify the readthrough behavior of E.                    coli's RNA polymerase.  An "N-Tester Plasmid" transcribes from                  IPTG-inducible ptac to a terminator (t) that blocks expression of               downstream reporter lacZ.  In the presence of N lambda and host                 cell Nus proteins, lacZ expression becomes activated by the                     insertion of an N recognition "nut" sequence between ptac and t.                The 5-base loop of the nut sequence, determining ability of N to                antiterminate, will be mutated exhaustively to determine the base               specificity at each position.  A larger effort will be needed to                understand the form of N protein, and the molecular basis for its               specific interactions at nut and with the host Nus proteins.  N                 mutations, located in a second plasmid compatible with N-Tester,                will be tested in vivo for function and specificity.  In the long               range, physical studies will augment genetic analysis of N                      protein from lambda, and N-analog proteins from lambda-related                  phages, proteins that share the antitermination function but                    differ in specificity.  The indication that N interacts with nut                when it is in its RNA transcript form will be tested by "gel                    retardation" of nut RNA and DNA during electrophoresis on                       nondenaturing gels.
{'FirstName': 'Naomi', 'LastName': 'Franklin', 'PI_MID_INIT': 'C', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Naomi C Franklin', 'EmailAddress': 'franklin@biology.utah.ed', 'NSF_ID': '000163388', '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': '1112', 'Text': 'Genetic Mechanisms'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1989&All=true', 'xml': '8900498.xml'}