Coding potential and regulatory signals of the polyoma virus genome

Soeda, Eiichi; Arrand, John R.; Smolar, Nina; Walsh, Jane E.; Griffin, Beverly E.

doi:10.1038/283445a0

Cited by 371 publications

(272 citation statements)

References 47 publications

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“…It should be noted that this truncation of the middle-T antigen removes the strongly hydrophobic sequence found near the carboxy terminus of the native protein. This single nucleotide deletion is the only change detected between the pPYY215 and the two different recovered plasmids (note that some differences from the published sequence [27] are also apparent, e.g. nucleotide 1217 will clearly be an A rather than a C ) but these changes are present in all three plasmids sequenced here and such changes from the published sequence have been observed previously in this laboratory.…”

Section: Sequence Analysis Of Plasmids Encoding the Truncated Middle-mentioning

confidence: 62%

Expression of polyoma virus middle-T antigen in Saccharomyces cerevisiae

1986

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The polyoma middle-T gene, lacking its intron, was inserted into a yeast expression plasmid containing the phosphoglycerate kinase promoter. Such plasmids transformed yeast at low frequency and these transformants expressed middle-T antigen at a level of approximately 0.1 % cell protein. Furthermore, expression of this protein was frequently lost during growth in liquid culture and this loss of middle-T was accompanied by a twofold increase in the rate of growth. The spontaneous production of a truncated middle-T antigen, lacking the C terminus, was also observed; the expression of this protein did not inhibit the growth rate of the cells. Recovery and analysis of the expression plasmids encoding the truncated molecule showed that a single C . G base pair had been deleted from a run of nine consecutive C . G base pairs (Pyr nucleotide 1239 -1247) within the middle-T coding region. This frame-shift mutation results in premature termination of the protein and loss of the strongly hydrophobic region of the molecule believed to be responsible for the membrane association of middle-T antigen.

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Section: Sequence Analysis Of Plasmids Encoding the Truncated Middle-mentioning

confidence: 62%

Expression of polyoma virus middle-T antigen in Saccharomyces cerevisiae

1986

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“…These were really pieces of work before their time. In 1978 two versions of complete nucleotide sequences (each over 5000 residues) of the papovavirus SV40 were published Reddy et al, 1978) and since then two other papovavirus genomes, BK and polyoma, have been analysed (Yang & Wu, 1979;Deininger et al, 1980;Soeda et al, 1980). Beginning in 1975, a trickle of adenovirus DNA sequence data has by now increased to a continuingflood (Steenbergh et aL, 1975;Arrand & Roberts, 1979;Akusj~irvi & Pettersson, 1979;Herisse et aL, 1980;van Ormondt et aL, 1980).…”

Section: The Fifth Fleming Lecture 3 History Of Nucleic Acid Sequencingmentioning

confidence: 99%

Structural Analysis of Animal Virus Genomes: The Fifth Fleming Lecture

McGeoch¹

1981

Journal of General Virology

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“…The abbreviations used are as those given in Table 1 ;IS well a s thc following: T K for thymidine kinase froin Ifcr,w~ .sinipic,.u virus [30]. NIT for the iron protein of nitrogenasc from C/o,\tridinn/ pas/c.r/riairiri?i [31], TSV40 for the large T-antigen protein o f simian virus 40 [32], TP0L.Y for the large T-antigen protein of polyonia virus [33], A D E N 0 for probable coat protein 2 of adeno-associated virus 2 [34] and TMVK for thc probable tobacco mosaic virus K N A replicating protein 1351. The sequence position of the lirst residue is indicated i n parentheses.…”

Section: Ydylvigggsgglasarraaelga---r\avvesklmentioning

confidence: 99%

Homologies and anomalies in primary structural patterns of nucleotide binding proteins

Argos¹,

Leberman²

1985

European Journal of Biochemistry

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In searches for homology among nucleotide binding proteins, recent reports have described primary structure alignments for stretches of 30 or so amino acid residues among a variety of proteins including the ray and oncogene products. The significance of these sequence matches has been tested by searching in available data banks for certain conserved residue patterns rcsulting from the alignments. The tests suggest that alignments over these limited stretches are not necessarily justifiable and any implications for residues involved in nucleotide binding must be viewed with caution.With recent advances in the technology of DNA sequencing, the primary structures of many proteins have been elucidated. 'This plethora of data has, probably because of the grcater effort and time required to obtain tertiary structural information, prompted searches for amino acid sequence homologies amongst proteins of known and unknown threedimensional structure. This is particularly so if the various proteins can be related by some common biochemical property. In cases where the sequence matches can be delineated for a 100 or more contiguous residues, with small and few insertions and deletions, the homology would appear significant. For other situations. only a short stretch of 15 to 35 amino acids in length has been reported for proteins consisting of 200 or more amino acids. Arguments for significance in these instances generally center on the alignment of such regions in scveral proteins with similar functions as well as a comparatively high perccntage of amino acid identity which is in the vicinity of 30-40%.Since many proteins bind nucleotides such a s GTP, ADP, or NAD and since conserved marker residues have been identified in the primary, secondary and tertiary structures of NAD-binding dehydrogenases [I ~ 31, there are many examplcs in the recent scientific literature suggesting nucleotide binding regions in proteins through alignment of short scquence spans. The current molecular biology interest in oncogene products has produced a wealth of amino acid scquence data and concomittant attempts to establish functional, structural or possibly evolutionary relationships between these proteins and non-oncogenic proteins of cstablished function and structure. I n this rcport homology studics of oncogene products which possess nucleotide binding properties will be considered: namely, thc rus group of proteins which bind GTP and the src group which bind ATP. By combining alignments from several recent reports through the use of common sequences (e. g. dehydrogenases), particular residue patterns were made salient. Searches of protein sc-

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Coding potential and regulatory signals of the polyoma virus genome

Cited by 371 publications

References 47 publications

Expression of polyoma virus middle-T antigen in Saccharomyces cerevisiae

Expression of polyoma virus middle-T antigen in Saccharomyces cerevisiae

Structural Analysis of Animal Virus Genomes: The Fifth Fleming Lecture

Homologies and anomalies in primary structural patterns of nucleotide binding proteins

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