Biology Reference
In-Depth Information
1 of reovirus.
Upper panel: Ribbon representations of P3A
(a)
, VP7A
(b)
, and
Fig. 3.
Comparison of P3 of RDV with VP7 of BTV and
λ
1A
(c)
,
viewed from the outside of the core particle. Lower panel: The same
images after rotation through 90
λ
°
.
To identify the role of the amino-terminal region of the P3 pro-
tein in the generation of RDV particles, our group produced a series
of deletion mutants of P3 with deletions of amino acids 2 through
10, 2 through 29, and 2 through 52 (N10del-P3, N29del-P3, and
N52del-P3, respectively). Then we analyzed the stability of the core
particles generated by these mutant proteins in the presence of high
concentrations of MgCl
2
.
9
Core-like particles (CLPs) were observed after expression of
N10del-P3 and of N29del-P3, but not after expression of N52del-P3,
thus indicating that the amino-terminal region from residue 30 to
residue 52 is essential for the self-assembly of core particles. A com-
parison of the structures of two of the deletion mutants of P3,
N29del-P3 and N52del-P3, revealed that N52del-P3 had lost the
α
-helical domain from residue 32 to residue 51, suggesting that the
amino acids in this region might be important for maintenance of
