Klessig, D. F., Grodzicker, T. (1979) Mutations that allow human Ad2 and Ad5 to express late genes in monkey cells map in the viral gene encoding the 72K DNA binding protein. Cell, 17 (4). pp. 957-966.
Abstract
Five host-range mutants (Ad2hr400-hr403, Ad5hr404) of human adenovirus serotype 2 and 5 (Ad2 and Ad5) which overcome the block to growth of wild-type adenovirus in [African green] monkey [kidney] cells were isolated. They form plaques and multiply efficiently in both monkey and human cells. The alteration in each of these mutants allows the full expression of all viral late genes, in marked contrast to the depressed synthesis of many late proteins in monkey cells infected with the parental Ad2 or Ad5. The altered gene encodes a diffusible product, since the mutation acts in trans to enhance the synthesis of wild-type Ad3 late proteins during co-infections of monkey cells with Ad2hr400 and Ad3. Restriction enzyme analysis of the genomes of all the host-range mutants show that none of them contain major alterations. In addition, an earlier report indicated that Ad2hr400 does not contain SV-40 sequences, which in some adenovirus-SV-40 hybrid viruses allows efficient multiplication in monkey cells. The mutation responsible for the extended host range was physically mapped by marker rescue experiments using isolated restriction enzyme fragments of the mutants to transfer the new phenotype to wild-type adenovirus. The alteration in each of the 5 mutants is located in a region (coordinates 62-70.7; coordinates 62-68 for Ad5hr404) which encodes predominantly the 72K [kilodalton] DNA binding protein. More detailed mapping using Ad2hr400 fragments places the mutation (coordinates 62.9-65.6) entirely within the 72K gene. The multifunctional nature of the 72K protein and some of its similarities to SV-40 T [tumor] antigen are discussed.
Item Type: | Paper |
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Subjects: | organism description > virus > adenovirus bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > mutations |
CSHL Authors: | |
Communities: | CSHL labs > Grodzicker Lab School of Biological Sciences > SBS Administration |
Depositing User: | Matt Covey |
Date: | 1979 |
Date Deposited: | 12 May 2016 20:44 |
Last Modified: | 09 Sep 2021 18:55 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/32701 |
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