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F Boschelli

Publications and source records attributed to F Boschelli.

6 recordsLinked to original sources
PubMed1989

Src homology 2 domain deletion mutants of p60v-src do not phosphorylate cellular proteins of 120-150 kDa.

We have constructed seven deletions in the src homology 2 (SH2) domain of the Rous sarcoma virus src gene and have expressed them and wild-type v-src (wt v-src) in Rat 1 fibroblasts. Transfected cells containing mutant DNAs have reduced focus forming activity when compared to cells containing the wt v-src DNA. In most cases, established cell lines that express these mutants have altered growth properties in soft agar. The src proteins isolated from mutant cell lines have reduced tyrosine kinase activity. We also see differences in the phosphorylation of cellular proteins in vivo. Unlike the wt protein kinase, the SH2 domain mutant kinases do not phosphorylate a set of cellular proteins ranging in size from 120-150 kDa.

Animals↗
PubMed1983

lambda Phage cro repressor interaction with DNA.

We present here the complete identification of the resonances from the aromatic region of the 1H NMR spectrum of the cro repressor of the Escherichia coli lysogenic phage lambda. This was accomplished by the use of two-dimensional NMR analysis as well as specifically deuterated tyrosines. Not surprisingly, it shows that the published resonance assignment approached by more conventional methods by others includes substantial errors. The effect of complex formation with DNA was examined in the 1H NMR spectrum as well as in 19F NMR spectra from 3-fluorophenylalanine- or 3-fluorotyrosine-substituted cro repressors. The fluoro analogues show the practicality of using a structural gene cloned into an inducible system as a starting point to obtain both material and specific nuclear spin incorporation for NMR spectroscopy. The NMR data offer direct support for the speculative models of cro repressor-DNA complexes proposed from x-ray structure analysis on the protein alone.

Bacteriophage lambda↗