Disease relevance of pol

• A joint produce of the genes gag and pol of avian sarcoma virus: a possible precursor of reverse transcriptase [1].
• Retroviral gag, pol and env gene products are translated as precursor polyproteins, which are cleaved by virus-encoded proteases to produce the mature proteins found in virions [2].
• Based on precedents from other retroviruses, the precursor of the human immunodeficiency virus (HIV-1) reverse transcriptase is predicted to be a polyprotein with a relative molecular mass (Mr) of 160,000 (160K) encoded by both the viral pol gene and the upstream gag gene [3].
• Major pol gene progenitors in the evolution of oncoviruses [4].
• Nucleotide sequence analysis revealed regions in the HLM-2 pol gene that were as much as 70 percent identical to the mouse mammary tumor virus pol gene [5].

High impact information on pol

• The gag gene is terminated by an amber stop codon and is contained within a different reading frame than is the pol gene [6].
• The pol and env genes overlap [6].
• A comparison of known protein sequences with the nucleotide sequence allows assignment of the coding regions for the gag, pol, env and src genes [6].
• These two genes lie in different translational reading frames, with the 3' end of gag overlapping the 5' end of pol by 205 or 241 nucleotides [3].
• Expression of the Rous sarcoma virus pol gene by ribosomal frameshifting [7].

Chemical compound and disease context of pol

• The HTLV-1 RT seems to be unique since its NH2 terminus is probably encoded by the pro open reading frame (ORF) fused downstream, via a transframe peptide, to the polypeptide encoded by the pol ORF [8].

Biological context of pol

• Furthermore, it was shown that the N-terminal ends of the M-MuLV pol product and the CaMV and 17.6 putative polymerases exhibit strong sequence homology with the gag-specific protease (p15) of Rous sarcoma virus (RSV) as well as the amino acid sequence predicted from the gag/pol spacer sequence of human adult T-cell leukaemia virus (HTLV) [9].
• Open reading frames for gag and pol genes were identified [10].
• Analysis of the primary structure of the long terminal repeat and the gag and pol genes of the human spumaretrovirus [10].
• The 5'-terminal half of the genomes (corresponding to the gag and pol regions) is virtually identical, with only scattered single nucleotide differences [11].
• DNA sequencing of the pol-src junction of BH-RSV revealed that the env sequence was almost entirely absent; only six base pairs following the pol termination codon remained [12].

Anatomical context of pol

• RNA analysis of nonproducer clones of RSV-29-infected chicken embryonic fibroblasts showed the presence of a subgenomic message of 2.6 kilobases containing src and a genomic RNA of 7.7 kilobases that contains gag, pol, and src, but not env [13].
• A 2-base substitution which created a nonsense mutation in the pol reading frame and was predicted to disrupt the hairpin structure of the ribosome frameshift signal had no effect on particle assembly or Gag processing, definitively showing that downstream amino acids are unnecessary [14].
• With the use of specific anti-RSV protein antisera, we found that only the viral gag and pol proteins were synthesized at levels similar to those synthesized in RSV-transformed fibroblasts; the synthesis of env and v-src proteins was significantly reduced in these infected myotubes [15].
• Two cell lines, H-18 and H-20, have all the viral structural genes expressed, but a new EcoRI recognition site appeared in the region of the pol gene sequence [16].

References