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Fig. 1. 2D-PAGE (10%) analysis of the N. crassa α-actinin and the GST-α-actinin constructs. A. A mixture of N. crassa crude extract and partially digested GST-α-actinin
fusion protein immunoblotted with anti-Neurospora α-actinin antibody. B. Diagrammatic representation of GST-α-actinin construction, bars underline the region of the protein reacting with the anti-Neurospora
α-actinin antibody shown in A. (GST, meansgluthathione S-transferase; CH, Calponin Homology domain; SR, spectrin repeat and EF, refers to EF-hand motif).
Fig. 2. Analysis of α-actinin-actin interactions. SDS-PAGE (10 %) coomassie blue
stained gel (upper panel) of supernatants (sn) and pellets (p) of α-actinin-actin mixtures and the corresponding immunoblot with the anti-actin antibody (lower panel). Lanes a, b and
c are 3.5 μM of G-actin, F-actin and GST-α-actinin respectively. Lanes d and erepresent reaction mixtures containing 3.5 μM actin and 2 μM (lane d) and 3.5 μM (lane
e) α-actinin. Lane f is the same as lane e but with excess calcium.Fig. 3. Electron micrographs of α-actinin-F-actin cross-reaction products. A. 2 μM
actin; B. α-actinin to actin molar ration 1:1 (2 μM); C. α-actinin to actin molar ratio 1:2 (1 μM:2 μM). Bar 100 nm.
Fig. 4. Calcium-binding of N. crassa α-actinin probed by calcium overlay using
45Ca. a, 10 μg of GST-α-actinin; b, α-actinin from chicken gizzard; c, calmodulin and d,
GST protein were slot-blotted onto a nitrocellulose membrane.
Fig. 5. Immunolocalization of N. crassa α-actinin during different stages of growth.
Germinating conidia, emerging germ tubes and growing hyphae corresponding to 1 hour (A) and 12 h (B-D) growth. Tip region of the hyphae with a branch initial (B).
Localization of α-actinin in the septum (C-D). Bar 5 μm.
Fig. 6. Time lapsed images of live cells for a duration of 5 hours. Laser scanning
confocal microscopy images of Neurospora hyphae expressing α-actinin-GFP. Images correspond to intervals of approximately 1 hour. After one hour of growth the fluorescence concentrated at the site of germination (A), this concentration was maintained until germ tube formation during the first 3 hours of growth (B-C), during hyphal growth no specific localization was found (D-E). The GFP signal accumulated at the fusion site of two hyphae (F). Bar 10 μm.
Fig. 7. In vivo localization of α-actinin in N. crassa. A-B. Transmission and GFP
signal is shown for each acquisition image; complete septum formation took less than 40 min. A. Time series corresponding to the first step of septum formation, the septum is not evident in the transmission images made during the first 20 min. B. Stack serie of the hyphae at 30 minutes, the fusion pore was visualized in the medial acquisition image. C.
confocal image showing a hyphal fusion using the transmission image (a), GFP signal (b)
Dans le document
Characterization of α-actinin as a member of the spectrin superfamily of proteins in "Neurospora crassa"
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