Abstract:
:The E8 open reading frame of bovine papillomavirus type 4 encodes a small hydrophobic polypeptide which contributes to cell transformation by conferring anchorage-independent growth. Using an in vitro translation system, we show that the E8 polypeptide binds to ductin, the 16-kDa proteolipid that forms transmembrane channels in both gap junctions and vacuolar H+-ATPase. This association is not due to nonspecific hydrophobic interactions. PPA1, a Saccharomyces cerevisiae polypeptide homologous (with 25% identity) to ductin, does not complex with E8. Furthermore, E5B, structurally similar to E8 but with no transforming activity, does not form a complex with ductin. Primary bovine fibroblasts expressing E8 show a loss of gap junctional intercellular communication, and it is suggested that this results from the interaction between E8 and ductin.
journal_name
J Viroljournal_title
Journal of virologyauthors
Faccini AM,Cairney M,Ashrafi GH,Finbow ME,Campo MS,Pitts JDdoi
10.1128/JVI.70.12.9041-9045.1996subject
Has Abstractpub_date
1996-12-01 00:00:00pages
9041-5issue
12eissn
0022-538Xissn
1098-5514journal_volume
70pub_type
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pub_type: 杂志文章
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