Identification and characterization of the genes encoding three structural proteins of the Sulfolobus virus-like particle SSV1 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-01

AUTHORS

Wolf-Dieter Reiter, Peter Palm, Agnes Henschen, Friedrich Lottspeich, Wolfram Zillig, Bernd Grampp

ABSTRACT

Three structural proteins, VP1, VP2 and VP3, of the virus-like particle SSV1 of the thermoacidophilic archaebacterium Sulfolobus sp. strain B12 were purified. VP1 and VP3 are very hydrophobic and show a high degree of homology. They consist of 73 and 92 amino acid residues, respectively. The third protein, VP2, is extremely basic containing 29 basic amino acids but only 4 acidic ones in a total of 74 amino acid residues. The genes encoding these three proteins were mapped within the genome by comparison of N-terminal amino acid sequences with the SSV1 DNA sequence. The three genes are closely linked in the order VP1-VP3-VP2 and the coding strand is the same in all three genes. Ten nucleotides separate the stop codon for VP1 from the initiation codon for VP3 and one nucleotide separates the genes encoding VP3 and VP2. Duplicate putative ribosome binding sites are found upstream of the initiation codons for VP2 and VP3. The major coat protein VP1 does not start with a methionine residue and appears to be the result of proteolytic cleavage of a precursor molecule. Transcription of the region encoding VP1, VP2 and VP3 results in the formation of two mRNAs of 0.5 kb and 1.0 kb, the shorter one only encoding VP1, the longer one spanning all three genes. A 61 bp sequence encoding part of VP1 is exactly repeated within the gene for VP3 and these identical sequences are translated into stretches of identical amino acids in the two proteins. A function of this repeated DNA sequence beyond its coding properties is very likely. More... »

PAGES

144-153

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    http://scigraph.springernature.com/pub.10.1007/bf00326550

    DOI

    http://dx.doi.org/10.1007/bf00326550

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