Shown is a schematic summary of macronuclear development in E.
crassus. Macronuclear-destined sequences are shown as black rectangles,
telomeres as hatched boxes, and IESs as ovals –see L. Klobutcher.
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Structural Biology
Shown is the recent NMR solution structure of the human XRCC1 NTD repair
protein (left, 1xna at the PDB) and a mechanism for interaction with a
human DNA polymerase beta-DNA complex (right, 1bpy at the PDB) –see G.
Mullen.
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Computational Biology and
Biophysics
The p16 protein is a cyclin dependent protein kinase inhibitor and a
tumor suppressor. The p16 structure (1BI7 from the PDB) consists of four
ankyrin repeats. Based on a computational analysis (bottom image) of the
autonomous folding units in p16, a C-terminal fragment (p16C) in red
containing only two ankyrin repeats (top image) has been identified and
shown by expression cloning, fragment production, and biophysical
characterization, to fold into a native-like structure. The plot shows
the Z-score (the higher the better for predicted complete folding) for
all possible peptide fragments that have the Y-axis value as the
N-terminal residue of the fragment and the X-axis value as the
C-terminal residue –see Z. Peng.
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Protein Biochemistry
Model of the protein architecture of the outer dynein arm showing
approximate positions of constituent light chains (LCs) and intermediate
chains (ICs) –see S. King.
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Cell Biology
Expression of Connexin 32-GFP fusion protein in oligodendrocytes.
Oligodendrocytes in culture were microinjected with RNA encoding a
Cx32-GFP fusion protein. The expressed protein was visualized by
confocal microscopy. The red indicates the distribution of Texas Red
dextran that was co-injected as a cytoplasmic marker. The green
indicates the distribution of Cx32-GFP fusion protein in numerous small
clusters throughout the cell. Experimental details are described in
Tedford et al. (1997) –see J. Carson.
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Microbial Physiology/Pathogenesis
Colocalization by immunofluorescence of a major vegetative cell
chromosomal protein (HBsu) with major spore DNA binding proteins (SASP)
in the developing spore (shown by the arrow)
of Bacillus subtilis –see P. Setlow.
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