Jl. Franklin et G. Mosig, EXPRESSION OF THE BACTERIOPHAGE-T4 DNA TERMINASE GENE-16 AND GENE-17 YIELDS MULTIPLE PROTEINS, Gene, 177(1-2), 1996, pp. 179-189
The products of the bacteriophage T4 terminase genes 16 and 17 are kno
wn to mediate cutting and packaging of concatemeric vegetative DNA. We
show here that the larger of these genes, 17, yields multiple protein
species. The complex expression of the T4 terminase genes includes ov
erlapping transcripts, probably initiated from multiple promoters, RNA
processing at certain preferred sites and translation initiation from
multiple ribosome binding sites (RES). Translation initiation from th
ese RES may be modulated by inverted repeat (IR) sequences whose foldi
ng can be predicted to differ in different RNA species. In T4 infected
bacteria, genes 16 and 17 are probably co-transcribed from several ne
ar-consensus late promoters upstream from gene 16, and processed at mu
ltiple sites. Additional 5' ends of late transcripts are located downs
tream from a near-consensus late promoter inside gene 17 and further d
ownstream, unrelated to any known promoter consensus sequence. The gen
e 17 transcripts that are initiated or cleaved internally contain RES
for shorter open reading frames (ORFs) in the same frame as full-lengt
h gene product (gp) 17 of 70 kDa. The truncated proteins, a 59-kDa gp1
7' and a 45-kDa gp17'', are synthesized from cloned gene 17 segments i
n which the first gene 17 RES is deleted. Expression of gene 17 is dif
ferent in BL21(DE3) or W3110[pACT7] host bacteria. The gp17' and gp17'
' proteins are predicted to contain one or more of the ATPase motifs t
hat are common among large subunits of other phage terminases. They la
ck a predicted single stranded (ss) DNA binding motif that is unique t
he large terminase proteins in T4 gp17, and that has been implicated i
n recognizing ssDNA regions in replicating and recombining T4 DNA dest
ined to be packaged. We hypothesize that a truncated gene 17' is an ev
olutionary precursor of the full-size T4 gene 17. Its function may hav
e been maintained to allow processive packaging from double stranded (
ds) DNA ends.