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Early region 1B of adenovirus 2 encodes two coterminal proteins of 495 and 155 amino acid residues

Journal Article · · J. Virol.; (United States)
OSTI ID:5006985

Partial sequence analysis of tryptic peptides has identified the E1B-495R (E1B-57K) (early transcription region 1B of 495 amino acid residues, with an approximate molecular weight of 57,000) protein of adenovirus 2 as encoded by the 495 amino acid open reading frame located in the adenovirus 2 DNA sequence between nucleotides 2016 and 3500. Additional proteins of 16,000 M/sub r/ and 18,000 M/sub r/ that are related to the E1B-495R protein were identified by cell-free translation of hybridization-selected mRNA. Analysis of (/sup 35/S)methionine-containing amino terminal tryptic peptides by thin-layer chromatography showed that the E1B-495R, E1B-18K, and E1B-16K proteins all begin at the same initiation codon. The E1B-495R protein from 293 cells also has the same initial tryptic peptide, acetyl-methionyl-glutamyl-arginine. Sequence analysis of E1B-18K tryptic peptides indicated that this protein also has the same carboxy terminus as the E1B-495R protein and that it is derived from an mRNA that is spliced to remove sequences between nucleotides 2250 and 3269, resulting in a protein product of 155 amino acid residues. Analysis of E1B-16K tryptic peptides has not yet revealed the carboxy terminal structure of this protein. Both the E1B-495R and the E1B-155R (E1B-18K) proteins, as well as the E1B-16K protein, were precipitated from cell-free translations and from extracts of infected cells by antiserum against an amino terminal nonapeptide common to these proteins.

Research Organization:
Brookhaven National Lab., Upton, NY
OSTI ID:
5006985
Journal Information:
J. Virol.; (United States), Journal Name: J. Virol.; (United States) Vol. 50:2; ISSN JOVIA
Country of Publication:
United States
Language:
English