ISSN:
1617-4623
Schlagwort(e):
φX174 gene E
;
Overlapping genes
;
Cell membrane
;
Gene fusion
;
Oligomerization
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
Notizen:
Summary Lytic activity of the φX174E (lysis) protein had previously been localized to the amino terminal 51 amino acids (a.a.) of the molecule (Blasi and Lubitz 1985). This E gene lytic activity has here been further localized to the amino terminal 29 a.a., a region of the protein which is thought to just span the cell membrane (Young and Young 1982). φX174 E gene fusions to both the lacZ gene and the chloramphenicol acetyl transferase (CAT) gene resulted in fusion proteins with lytic activity. Fusion to a third protein, trpE, did not result in lytic activity. These results support a model of oligomerization of the φX174 E protein for lytic activity since both β-galactosidase and CAT exist as tetramers in their native state. A difference in the composition of the charged amino acids at the cytoplasmic boundary between the various fusion proteins could also account for these results, since these amino acids may play a role in proper anchoring of the E protein in the cell membrane. In a spontaneous E gene mutant, which introduces a proline residue at position 9 of the E protein, lytic activity of the E protein was decreased, but not abolished. The presence of the helix-breaking proline at this position may interfere with insertion of the lysis protein into the cell membrane, leading to the decreased functional activity of the protein.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00330198
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