Peter Gauss
University of Colorado Boulder
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Featured researches published by Peter Gauss.
Cell | 1982
Britta Swebilius Singer; Larry Gold; Peter Gauss; Daniel H. Doherty
Homology is an important feature of recombination. We have used the rll cistrons of bacteriophage T4 to determine the extent of homology required for recombination. We varied the amount of homologous DNA available for recombination in both marker rescue experiments and deletion-by-deletion crosses. Our results suggest that the primary pathway for recombination in T4 requires 50 bp of homology. Our finding that recombination is detectable when fewer than 50 bp of homology are available suggests that there is a second, less efficient pathway of recombination in T4. This pathway may be used during the formation of deletions.
Journal of Molecular Biology | 1987
Eric S. Miller; Jim Karam; Myra M. Dawson; Maria Trojanowska; Peter Gauss; Larry Gold
The RegA protein of bacteriophage T4 is a translational repressor that regulates expression of several phage early mRNAs. We have cloned wild-type and mutant alleles of the T4 regA gene under control of the heat-inducible, plasmid-borne leftward promoter (PL) of phage lambda. Expression of the cloned regA+ gene resulted in the synthesis of a protein that closely resembled phage-encoded RegA protein in biological properties. It repressed its own synthesis (autogenous translational control) as well as the synthesis of specific T4-encoded proteins that are known from other studies to be under RegA-mediated translational control. Cloned mutant alleles of regA exhibited derepressed synthesis of the mutant regA gene products and were ineffective in trans against RegA-sensitive mRNA targets. The effects of plasmid-encoded RegA proteins were also demonstrated in experiments using two compatible plasmids in uninfected Escherichia coli. The two-plasmid assays confirm the sensitivities of several cloned T4 genes to RegA-mediated translational repression and are well-suited for genetic analysis of RegA target sites. Repression specificity in this system was demonstrated by using wild-type and operator-constitutive translational initiation sites of T4 rIIB fused to lacZ. The results show that no additional T4 products are required for RegA-mediated translational repression. Additional evidence is provided for the proposal that uridine-rich mRNA sequences are preferred targets for the repressor. Surprisingly, plasmid-generated RegA protein represses the synthesis of some E. coli proteins and appears to enhance selectively the synthesis of others. The RegA protein may have multiple functions, and its binding sites are not restricted to phage mRNAs.
Molecular Genetics and Genomics | 1987
Peter Gauss; Margit Gayle; Robert B. Winter; Larry Gold
SummaryWe have cloned and sequenced a bacteriophage T4 EcoRI fragment that complements T4 del (39-56) infections of an optA defective Escherichia coli strain. Bacteria containing this recombinant plasmid synthesize two new proteins with molecular weights of 9 and 26 kilodaltons. We have identified the gene encoding the 26 kilodalton protein as essential for T4 infections of optA defective E. coli. Genetic and biochemical results are consistent with the identification of this protein as the product of the dexA gene, which encodes a 3′ to 5′ exonuclease.
Molecular Microbiology | 1989
S. Quirk; D. Seto; S. K. Bhatnagar; Peter Gauss; Larry Gold; Maurice J. Bessman
The structural gene for deoxyguanosine triphosphate triphosphohydrolase (dGTPase) (EC 3.1.5.1) and its regulator, optA, have been located on a lambda phage carrying a 17.5kb Escherichia coli DNA insert. The DNA fragment has been excised and ligated into pBR325 and also transferred to another lambda vector. From the results of transduction and transformation experiments, we find that the structural gene for dGTPase is very closely linked to optA and dapD, which locates it at approximately 3.6 minutes on the genetic map of E. coli K12. We propose the mnemonic dgt as the designation for the structural gene for this enzyme.
Archive | 1982
Daniel H. Doherty; Peter Gauss; Larry Gold
SummaryThe product of gene 32 of bacteriophage T4 is a single-stranded DNA binding protein involved in T4 DNA replication, recombination and repair. Functionally differentiated regions of the gene 32 protein have been described by protein chemistry. As a preliminary step in a genetic dissection of these functional domains, we have isolated a large number of missense mutants of gene 32. Mutant isolation was facilitated by directed mutagenesis and a mutant bacterial host which is unusually restrictive for missense mutations in gene 32. We have isolated over 100 mutants and identified 22 mutational sites. A physical map of these sites has been constructed and has shown that mutations are clustered within gene 32. The possible functional significance of this clustering is considered.
Proceedings of the National Academy of Sciences of the United States of America | 1988
C Tuerk; Peter Gauss; C Thermes; Duncan R. Groebe; M Gayle; Nancy Guild; Gary D. Stormo; Y d'Aubenton-Carafa; Olke C. Uhlenbeck; I Tinoco
Proceedings of the National Academy of Sciences of the United States of America | 1987
R B Winter; L Morrissey; Peter Gauss; Larry Gold; T Hsu; Jim Karam
Proceedings of the National Academy of Sciences of the United States of America | 1983
Peter Gauss; Daniel H. Doherty; Larry Gold
Proceedings of the National Academy of Sciences of the United States of America | 1987
Peter Gauss; K B Krassa; David S. McPheeters; Michele Nelson; Larry Gold
Molecular Genetics and Genomics | 1982
Daniel H. Doherty; Peter Gauss; Larry Gold