Matches in SemOpenAlex for { <https://semopenalex.org/work/W1940400153> ?p ?o ?g. }
- W1940400153 endingPage "4602" @default.
- W1940400153 startingPage "4590" @default.
- W1940400153 abstract "The herpes simplex virus type 1 (HSV-1) alpha or immediate-early proteins ICP4 (IE175), ICP0 (IE110), and ICP27 (IE63) are trans-acting proteins which affect HSV-1 gene expression. We previously showed that ICP27 in combination with ICP4 and ICP0 could act as a repressor or an activator in transfection assays, depending on the target gene (R. E. Sekulovich, K. Leary, and R. M. Sandri-Goldin, J. Virol. 62:4510-4522, 1988). To investigate the regions of the ICP27 protein which specify these functions, we constructed a series of in-frame insertion and deletion mutants in the ICP27 gene. These mutants were analyzed in transient expression assays for the ability to repress or to activate two different target genes. The target plasmids used consisted of the promoter regions from the HSV-1 beta or early gene which encodes thymidine kinase and from the beta-gamma or leaky late gene. VP5, which encodes the major capsid protein, each fused to the chloramphenicol acetyltransferase gene. Our previous studies showed that induction of pTK-CAT expression by ICP4 and ICP0 was repressed by ICP27, whereas the stimulation of pVP5-CAT expression seen with ICP4 and ICP0 was significantly increased when ICP27 was also added. In this study, a series of transfection assays was performed with each of the ICP27 mutant plasmids in combination with plasmids containing the ICP4 and ICP0 genes with each target. The results of these experiments showed that mutants containing insertions or deletions in the region from amino acids 262 to 406 in the carboxy-terminal half of the protein were unable to stimulate expression of pVP5-CAT but were able to repress induction of pTK-CAT activity by ICP4 and ICP0. Mutants in the carboxy-terminal 78 amino acids lost both activities; that is, these mutants did not show repression of pTK-CAT activity or stimulation of pVP5-CAT activity, whereas mutants in the hydrophilic amino-terminal half of ICP27 were able to perform both functions. These results show that the carboxy-terminal half of ICP27 is important for the activation and repression functions. Furthermore, the carboxy-terminal 62 amino acids are required for the repressor activity, because mutants with this region intact were able to repress. Analysis of the DNA sequence showed that there are a number of cysteine and histidine residues encoded by this region which have some similarity to zinc finger metal-binding regions found in other eucaryotic regulatory proteins. These results suggest that the structural integrity of this region is important for the function of ICP27." @default.
- W1940400153 created "2016-06-24" @default.
- W1940400153 creator A5002805151 @default.
- W1940400153 creator A5049742945 @default.
- W1940400153 creator A5056348577 @default.
- W1940400153 creator A5060028603 @default.
- W1940400153 creator A5084666921 @default.
- W1940400153 date "1989-11-01" @default.
- W1940400153 modified "2023-10-16" @default.
- W1940400153 title "The regions important for the activator and repressor functions of herpes simplex virus type 1 alpha protein ICP27 map to the C-terminal half of the molecule" @default.
- W1940400153 cites W123433535 @default.
- W1940400153 cites W1484990013 @default.
- W1940400153 cites W1490731141 @default.
- W1940400153 cites W1496779362 @default.
- W1940400153 cites W1511816912 @default.
- W1940400153 cites W1516191360 @default.
- W1940400153 cites W1546196149 @default.
- W1940400153 cites W1559441251 @default.
- W1940400153 cites W1567938941 @default.
- W1940400153 cites W1570853101 @default.
- W1940400153 cites W1576021204 @default.
- W1940400153 cites W1580232960 @default.
- W1940400153 cites W1583466448 @default.
- W1940400153 cites W1606171762 @default.
- W1940400153 cites W1645759506 @default.
- W1940400153 cites W1667125802 @default.
- W1940400153 cites W1733825645 @default.
- W1940400153 cites W1751881098 @default.
- W1940400153 cites W1763401036 @default.
- W1940400153 cites W1768938879 @default.
- W1940400153 cites W177007720 @default.
- W1940400153 cites W1807108043 @default.
- W1940400153 cites W1817074176 @default.
- W1940400153 cites W1818730568 @default.
- W1940400153 cites W1820557301 @default.
- W1940400153 cites W1834346265 @default.
- W1940400153 cites W1880978891 @default.
- W1940400153 cites W1891768184 @default.
- W1940400153 cites W1931233319 @default.
- W1940400153 cites W1964297270 @default.
- W1940400153 cites W1964857093 @default.
- W1940400153 cites W1971290197 @default.
- W1940400153 cites W1971436037 @default.
- W1940400153 cites W1979281102 @default.
- W1940400153 cites W1986352563 @default.
- W1940400153 cites W1993028041 @default.
- W1940400153 cites W2003624865 @default.
- W1940400153 cites W2003638865 @default.
- W1940400153 cites W2004925049 @default.
- W1940400153 cites W2010356985 @default.
- W1940400153 cites W2018289835 @default.
- W1940400153 cites W2019332162 @default.
- W1940400153 cites W2023686279 @default.
- W1940400153 cites W2024810195 @default.
- W1940400153 cites W2033858354 @default.
- W1940400153 cites W2037653294 @default.
- W1940400153 cites W2040003193 @default.
- W1940400153 cites W2046261180 @default.
- W1940400153 cites W2048327622 @default.
- W1940400153 cites W2050210485 @default.
- W1940400153 cites W2053796273 @default.
- W1940400153 cites W2056650797 @default.
- W1940400153 cites W2058060471 @default.
- W1940400153 cites W2059823369 @default.
- W1940400153 cites W2060131368 @default.
- W1940400153 cites W2060993851 @default.
- W1940400153 cites W2063798194 @default.
- W1940400153 cites W2066276180 @default.
- W1940400153 cites W2067769780 @default.
- W1940400153 cites W2069892944 @default.
- W1940400153 cites W2070134552 @default.
- W1940400153 cites W2070921566 @default.
- W1940400153 cites W2071482027 @default.
- W1940400153 cites W2073073419 @default.
- W1940400153 cites W2073548049 @default.
- W1940400153 cites W2078157295 @default.
- W1940400153 cites W2088167128 @default.
- W1940400153 cites W2092743487 @default.
- W1940400153 cites W2095557476 @default.
- W1940400153 cites W2098074102 @default.
- W1940400153 cites W2101108802 @default.
- W1940400153 cites W2110360181 @default.
- W1940400153 cites W2119232680 @default.
- W1940400153 cites W2124100270 @default.
- W1940400153 cites W2132417094 @default.
- W1940400153 cites W2144902489 @default.
- W1940400153 cites W2146398256 @default.
- W1940400153 cites W2148633495 @default.
- W1940400153 cites W2149606427 @default.
- W1940400153 cites W2153414536 @default.
- W1940400153 cites W2154332606 @default.
- W1940400153 cites W2157911990 @default.
- W1940400153 cites W2159545772 @default.
- W1940400153 cites W2160637804 @default.
- W1940400153 cites W2161043652 @default.
- W1940400153 cites W2163403783 @default.
- W1940400153 cites W2166195788 @default.
- W1940400153 cites W2167414261 @default.