Small fragments of herpesvirus DNA with transforming activity contain insertion sequence-like structures.

Galloway, Denise A.; Nelson, Jay A.; McDougall, James K.

doi:10.1073/pnas.81.15.4736

Cited by 66 publications

(48 citation statements)

References 38 publications

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“…Our analysis of HCMV lytically infected cells has identified two mtrII-specific RNA transcripts large enough to code for the 70-, 83-, and 34-residue polypeptides. The mtrll domain also contains secondary structural elements-i.e., stemloops-similar to those found in other herpesvirus transforming domains (3,21). The sequence analysis of the mtrII domain revealed sequence elements upstream of the ORFs that are characteristic of a promoter.…”

Section: Discussionsupporting

confidence: 76%

“…Transforming domains among the herpesviruses have been localized in small DNA fragments (2,3,21). To date, no nuclease analysis were performed as described previ-_P4 ously (20 transforming polypeptide has been identified in HCMVinduced transformation.…”

Section: Discussionmentioning

confidence: 99%

“…pCM4127 DNA was reported to cause one-step focal transformation of primary Wistar rat embryo cells and NIH 3T3 mouse cells (1,2). This sequence was noncoding and contained a stem-loop structure (3) analogous to an insertion-like element.…”

mentioning

confidence: 99%

“…These data suggested that EM sequences were required both to initiate and to maintain the transformed phenotype. In contrast, EJ sequences were required only for the initiation of transformation, perhaps by a hit-and-run mechanism analogous to the BglII-N fragment of herpes simplex virus 2 or pCM4127 of HCMV AD169 (3).…”

mentioning

confidence: 99%

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Localization and DNA sequence analysis of the transforming domain (mtrII) of human cytomegalovirus.

Razzaque

Jahan

McWeeney

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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To define the morphological transforming region II (mtrl) of human cytomegalovirus (HCMV), a series of subclones of the Xba I/BamHI fragment EM was constructed in vitro and tested for focus-forming activity and tumorigenicity. A 980-base-pair subclone of fragment EM was identified, and its nucleotide sequence revealed three small open reading frames (ORFs), encoding 79, 83, and 34 amino acid residues. Si nuclease analysis of HCMV-infected cells DNA of human cytomegalovirus (HCMV) contains three transforming fragments, which have been mapped in the long unique region of the viral genome (see Fig. 1 Left). A minimal region of 558 base pairs (bp) (pCM4127) was localized in the Xba 1/HindIII fragment of HCMV strain AD169 (map unit 0.123-0.140) and designated morphological transforming region I (mtri). pCM4127 DNA was reported to cause one-step focal transformation of primary Wistar rat embryo cells and NIH 3T3 mouse cells (1, 2). This sequence was noncoding and contained a stem-loop structure (3) analogous to an insertion-like element.Two distinct transforming regions were mapped in the 20-kilobase (kb) Xba I fragment E (XbaI-E) of HCMV Towne DNA (map unit 0.680-0.770). Cloned XbaI-E will immortalize diploid Syrian hamster embryo cells and induce the neoplastic transformation of established rodent cell lines (4). The left-hand 3-kb Xba I/BamHI EM segment of XbaI-E, designated mtrII, and a right-hand 7.6-kb Xba I/BamHI EJ segment, designated mtrIII, were independently capable of inducing tumorigenic transformation of established rodent cells (5). Cell lines transformed individually by EJ or EM and their tumor derivatives retained the EM but not the EJ sequence (5). Similarly, only EM sequences were retained in the transformed and tumor-derived cells induced by cotransfection of cloned EJ and EM plasmids (unpublished data). These data suggested that EM sequences were required both to initiate and to maintain the transformed phenotype. In contrast, EJ sequences were required only for the initiation of transformation, perhaps by a hit-and-run mechanism analogous to the BglII-N fragment of herpes simplex virus 2 or pCM4127 of HCMV AD169 (3).In the present study we localized a minimal 980-bp transforming Ban II-Xho I region within the HCMV Towne Xba I/BamHI EM fragment and determined its nucleotide sequence. ¶ Nucleotide sequence analysis identified three potential open reading frames (ORFs) within the 980-bp fragment, and S1 nuclease protection assay revealed the presence of "early" RNA transcripts in infected cells. In addition, noncoding DNA sequence elements were observed with the potential to form stem-loop structures.

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Section: Discussionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Localization and DNA sequence analysis of the transforming domain (mtrII) of human cytomegalovirus.

Razzaque

Jahan

McWeeney

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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“…Comparable mutation frequencies have been obtained in six individual experiments. Similar IS-like structures, endowed with mutagenic activity, were detected in the transforming region of the genomes of herpes simplex virus type 2 and cytomegalovirus (Galloway et al, 1984;Brandt et al, 1987). To test the enhancer activity in transformation, BKV-IR or BKV-WT HindlII fragment C were placed upstream of the activated human c-ras oncogene and the recombinants were transfected into Rat-1 cells.…”

mentioning

confidence: 93%

Characterization of BK virus variants rescued from human tumours and tumour cell lines

Negrini

Rimessi²,

Mantovani³

et al. 1990

Journal of General Virology

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Cell Differentiation and Tumour Suppression

Sachs

2007

Ciba Foundation Symposium 142 ‐ Genetic Analysis of Tumour Suppression

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Small fragments of herpesvirus DNA with transforming activity contain insertion sequence-like structures.

Cited by 66 publications

References 38 publications

Localization and DNA sequence analysis of the transforming domain (mtrII) of human cytomegalovirus.

Localization and DNA sequence analysis of the transforming domain (mtrII) of human cytomegalovirus.

Characterization of BK virus variants rescued from human tumours and tumour cell lines

Cell Differentiation and Tumour Suppression

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