Biology Reference
In-Depth Information
although stronger evidence is needed to positively classify these as
amyloid. Collectively, these discoveries led to the functional amyloid
hypothesis, which states that organisms have evolved to take
advantage of the predisposition of polypeptides to form amyloid,
despite the fact that amyloid can be toxic. Thus, the amyloid fold is
a structural motif that can be adapted to serve a variety of functions
analogous to other folds including the
β
-sandwich,
β
-barrel folds.
Table 1.2
Known functional amyloid proteins
Kingdom
Species
Protein
Function
Supporting data
36
36,37
Bacteria
Escherichia coli
,
Curli
Biofilm formation,
host invasion
EM,
CR,
36
36,37
Salmonella
spp.
ThT,
CD
23
23
23
Streptomyces
coelicolor
Chaplins
Modulation of
water surface
tension
CD,
ThT,
EM
38,39
38,39
Fungi
Podospora
anserine
Het-s
Regulation of
heterokaryon
formation
EM,
CD,
38,39
38
FTIR,
CR,
40
NMR
41
41
Saccharomyces
cerevisiae
URE2p
Regulation
of nitrogen
catabolism
ED,
X-Ray,
24
24
42
CR,
EM,
ThT
43
43
S. cerevisiae
Rnq1p
Unknown
ThT,
EM
25
25
25
S. cerevisiae
Sup35p
Regulation of
stop-codon read-
through
EM,
CR,
CD,
44
X-ray
26,45
26,45
Most fungi
Hydrophobins Fungal coat
formation,
modulation of
adhesion and
surface tension
AFM,
CD,
45
28,45
FTIR,
ThT,
26,35
26,28
NMR,
CR,
35
X-ray
Animalia Insects and fish Chorion
proteins
Structural and
protective
functions in the
eggshell
CR,
46,47
X-ray,
29,46
EM,
29,46,47
FTIR,
46,47
CD
47
48
48
Nephila clavipes
Spidroins
Structural
— spider silk
EM,
CD
32
32
Homo sapiens
Pmel17
Melanin
biosynthesis
X-Ray,
CR,
32
32
EM,
ThT
CD, ultraviolet circular dichroism spectroscopy; CR, Congo red
binding; ED, electron diffraction; EM, electron microscopy; FTIR,
Fourier-transform infrared spectroscopy; NMR, nuclear magnetic
resonance spectrometry; ThT, thioflavin T binding; X-ray = X-Ray
diffraction.
Search WWH ::
Custom Search