Autor: |
Norihito Ohta, John F. Atkins, Hirokazu Morisawa, Tohru Nishihara, Yukinobu Nishimura |
Rok vydání: |
2004 |
Předmět: |
|
Zdroj: |
Genes to Cells. 9:877-889 |
ISSN: |
1356-9597 |
DOI: |
10.1111/j.1365-2443.2004.00778.x |
Popis: |
The maturation/lysis (A2) protein encoded by the group B single-stranded RNA bacteriophage Qbeta mediates lysis of host Escherichia coli cells. We found a frameshift mutation in the replicase (beta-subunit) gene of Qbeta cDNA causes cell lysis. The mutant has a single base deletion 73 nucleotides (nt) 3' from the start of the replicase gene with consequent translation termination at a stop codon 129-131 nt further 3'. The 43-amino acid C-terminal part of the 67-amino acid product encoded by what in WT (wild-type) is the +1 frame, is rich in basic amino acids This 67-aa protein can mediate cell lysis whose characteristics indicate that the protein may cause lysis by a different mechanism and via a different target, than that caused by the A2 maturation/lysis protein. Synthesis of a counterpart of the newly discovered lysis product in wild-type phage infection would require a hypothetical ribosomal frameshifting event. The lysis gene of group A RNA phages is also short, 75 codons in MS2, and partially overlaps the first part of their equivalently located replicase gene, raising significant evolutionary implications for the present finding. |
Databáze: |
OpenAIRE |
Externí odkaz: |
|