147 research outputs found
MUTATIONS IN THE VP1 CODING REGION OF POLYOMAVIRUS DETERMINE DIFFERENTIATING STAGE SPECIFICITY
Polyomavirus mutants capable of replicating in undifferentiated murine C2 myoblasts were selected and characterized. These mutants grow normally in 3T6 mouse fibroblast cells, and they do not complement the wild-type virus in coinfection experiments of C2 myoblasts. Of 12 isolates, 10 possess duplications of the regulatory region including the enhancer A domain. On the bases of the regulatory region structure and the presence and length of the enhancer duplication, the mutant viruses could be grouped into three classes. One mutant class (e.g., PyMB3) possesses an enhancer duplication of 91 bp identical to that of a previously characterized polyomavirus mutant, PyNB11/1. We have demonstrated that this enhancer duplication gives rise at its junction to a novel recognition motif for the transcriptional factor NF-1 (M. Caruso, C. Iacobini, C. Passananti, A. Felsani, and P. Amati, EMBO J. 9:947-955, 1990). The regulatory region PyMB3 virus recombined in a wild-type genome context maintains the mutant phenotype. The other two types of mutants, one with a 30-bp enhancer duplication (e.g., PyMB40) and one with a wild-type enhancer structure (e.g., PyMB27), possess two similar but distinct 6-bp deletions in the same region of the VP1 coding gene. In both cases, the ability to replicate in undifferentiated C2 myoblasts is strictly correlated to the mutation in the VPI coding region
Le società a partecipazione pubblica tra diritto dell’impresa e diritto dell’amministrazione. Una riflessione di apertura
Le società a partecipazione pubblica tra diritto dell’impresa e diritto dell’amministrazione. Una riflessione di apertura
Human p300 protein is a coactivator for the transcription factor MyoD
Human p300 protein is a cellular target of adenoviral E1A oncoprotein and a potential transcriptional coactivator. Both p300 and Rb family protein- binding regions of E1A are required for the repression of muscle gene expression, which is regulated by MyoD family transactivators. This implies that p300 is involved in MyoD-dependent transactivation. We show that the repression of MyoD-mediated E box (MyoD consensus) reporter activity by E1A is correlated with its interaction with p300, indicating that p300 participates in MyoD-dependent transactivation. In addition, p300 is able to interact both in vivo and in vitro with MyoD through a portion at the carboxyl-terminal cysteine/histidine-rich domain and associates with the components of the basal transcriptional complex through its two separate transactivation domains at the amino and carboxyl termini. Consistent with its role as a coactivator, p300 potentiates MyoD-activated transcription
Oligopeptides impairing the Myc-Max heterodimerization inhibit lung cancer cell proliferation by reducing Myc transcriptional activity
Deregulated CMYC gene causes cell transformation and is often correlated with tumor progression and a worse clinical outcome of cancer patients. The transcription factor Myc functions by heterodimerizing with its partner, Max. As a strategy to inhibit Myc activity, we have synthesized three small peptides corresponding to segments of the leucine zipper (LZ) region of Max. The purpose of these peptides is to occupy the site of recognition between Myc and Max located in the LZ and inhibit-specific heterodimerization between these proteins. We have used the synthesized oligopeptides in two lung cancer cell lines with different levels of Myc expression. Results demonstrate that: (i) the three peptides resulted equally effective in competing the interaction between Myc and Max in vitro; (ii) they were efficiently internalized into the cells and significantly inhibited cell growth in the cells showing the highest Myc expression; (iii) one specific peptide, only nine aminoacids long, efficiently impaired the transcriptional activity of Myc in vivo, showing a more stable interaction with this protein. Our results are relevant to the development of novel anti-tumoral therapeutic strategies, directed to Myc-overexpressing tumors
Organizzazione della Rai s.p.a.: pluralismo del servizio pubblico e "primato" del consiglio di amministrazione
Expression in male and genomic organization of the gene(s) coding for a major protein secreted by the rat seminal vesicle epithelium
Double strand cDNA copies of lls poly(A)+mRNA purified from adult rat seminal vesicles (RSV), have been cloned in E.coli C600 using the Pst I site of pBR322. Filter hybridization, nucleotide sequence analysis and positive hybridization translation were used to demonstrate that one of the recombinant plasmids obtained (pRSV25) contained a 260 bp long insert coding for a significant part of the precursor to the protein IV present in the RSV secretion. By using labelled pRSV25 DNA we have found that high levels of RSV IV mRNA were present only in the rat seminal vesicle epithelium. The amounts of RSV IV mRNA present in other tissues of the same organism were below the levels detectable by the methods used. In addition, other data reported here indicate that the RSV IV gene(s) is present in both sexes, probably with a different organization
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