Figure 6.

(A) Delayed aerial hyphae formation of chpA,C,D,H and chpA,B,C,D,H

strains, compared with the wild-type strain, M600, when grown on MS agar. (B)
Scanning electron microscope images of M600, chpA,C,D,H and chpA,B,C,D,H
after growth for 4 d on MS agar
Figure 3. Expression profiles of the chaplin genes in the bldN mutant strain and its
congenic parent, J1915. The color representation is as described in the legend for
Figure 1A.
Figure 1. A model showing the A. tumefaciens VirB/D4 T4SS as a single,
supramolecular organelle. The VirD4 CP is a homomultimeric integral membrane
complex required for substrate transfer.TheVirB proteins assemble as a secretion
channel and an extracellular T pilus. VirD4 and the VirB proteins function together
to mediate substrate transfer, and the VirB proteins direct pilus assembly. The
adhesive T pilus at the cell surface is postulated to promote aggregation of donor
and recipient cells on solid surfaces. IM, inner membrane; P, periplasm; OM,
outer membrane. Reprinted with permission from: Christie PJ. Biochim Biophys
Acta 2004;
Figure 2. Possible architectures and substrate transloction routes for the T4SS.
Numbers refer to VirB/VirD proteins of the Agrobacterium T-DNA transport
system. Three working models describe the possible machine architectures and
translocation routes: (1) a one-step model using a transenvelope channel, (2) a
two-step model using the T4CP or alternative translocase for substrate transfer
across the inner membrane (IM) and the mpf complex for outer membrane (OM)
translocation, and (3) another two-step model, the “shoot and pump model”,
whereby theT4CP recruits substrates and transports DNA across the IM and
delivers protein substrates to the mpf protein export machinery. Blue line,T-
strand; red circle, relaxase bound to theT-strand; green circle, protein substrate;
P, periplasm. Reprinted with permission from: Ding Z, Atmakuri K, Christie PJ.
Trends Microbiol 2003; 11:527-535.©2003 Elsevier.
Schematic drawing showing the formation of
oriented functional S-layer lattices on
peptidoglycan-containing sacculi and artificial
supports coated with secondary cell wall polymer.
In the case of peptidoglycan-containing sacculi,
only the outer S-layer is shown.
FIG. 8.
Electron micrographs of negatively stained preparations. (a) Self-assembly
properties of rSbpA. (b) Ability of rSbpA to recrystallize on poly- -lysine-coated EM grids. (c)
l

Formation of the square S-layer lattice by rSbpA

31-1068
/Bet v1 on peptidoglycan-containing sacculi of B.
sphaericus CCM 2177. (d) Immunogold labeling of recrystallization products
obtained with rSbpA31-1068/Bet v1 using the Bet v1-specific monoclonal antibody
BIP1. Bars, 200 nm.
Self-assembly products and digital image reconstructions of SbsB (see A and
C for comparison) and fusion protein (S1)3S1B1 (B and D). (A and B) The
crystalline sheets were formed in suspension and negatively stained with
uranyl acetate for TEM. The arrows indicate the base vectors of the oblique p1
lattice. (Bars = 50 nm.) (C and D) The digital image reconstructions were
made by Fourier processing of electron micrographs (not identical to the ones
shown in A and B). The region of highest protein mass in the SbsB lattice is
the SLH-domain (C, arrow). In the lattice of the fusion protein, streptavidin
showed up as additional protein mass (D, thick arrow) attached to the SLH
domain. (Bars = 10 nm.)
Proc Natl Acad Sci U S A. 2002 November 12; 99(23): 14646–14651.
Published online 2002 November 4. doi: 10.1073/pnas.232299399.
Copyright © 2002, The National Academy of Sciences
Applied Biological Sciences
S-layer-streptavidin fusion proteins as template for nanopatterned
molecular arrays
Dieter Moll, Carina Huber, Birgit Schlegel, Dietmar Pum, Uwe B. Sleytr,
and Margit Sára*
Center for Ultrastructure Research and Ludwig Boltzmann Institute for
Molecular Nanotechnology, University of Agricultural Sciences, A-1180
Vienna, Austria