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Peridinin-chlorophyll a proteins of dinoflagellate algae. [Role in photosynthesis]

TL;DR: The peridinin-chlorophyll a proteins from dinoflagellates examined were found to exist in a unique and distinctive pattern as shown by isoelectric focusing on polyacrylamide gel, of value for species identification and provide a biochemical marker for a particular species.
Abstract: The pigments which function as the energy collection systems for photosynthesis are either tetrapyrroles or carotenoids. In the oceans, which cover over 70 percent of the surface of the earth, carotenoids may be more important than chlorophylls for photosynthetic energy capture by phytoplankton. A characteristic feature of the principal marine phytoplankton is the possession of a high carotenoid content. In general each major group of phytoplankton has a specific carotenoid which accounts for a major portion of the total carotenoid content. The peridinin-chlorophyll a proteins from dinoflagellates examined were found to exist in a unique and distinctive pattern as shown by isoelectric focusing on polyacrylamide gel. These patterns may be of value for species identification and provide a biochemical marker for a particular species. To date, no similar proteins have been isolated from other phytoplankton groups.

Summary (1 min read)

INTRODUCTION

  • The pigments which function as the energy collection systems for photosynthesis are either tetrapyrroles or carotenoids.
  • In the oceans, which cov~r over 70% of the surface of the earth, carotenoids may be more important than chlorophylls for photosynthetic energy capture by phytoplankton.
  • The accessory pigment function of fucoxanthin and peridinin A pure culture of the alga was obtained by the use of agar p.lating a.nd antiobiotics.
  • .; -4-Large scale axenic cultures were maintained by using autoclaved or pasteurized media and antibiotics.
  • Recently, the authors found that aeration with 0.1% co 2 improved the growth of A. carterae and several other dinoflagellate algae.

PROPERTIES OF THE PERIDININ-CHLOROPHYLL A PROTEINS

  • When the Sephadex G-100 eluate was subjected to isoelectric focusing on polyacrylamide gel, it separated into six distinct components (Fig. 2 ). each separated component had absorbance which can be attributed to peridinin and chlorophyll !.
  • All peridinin-chlorophyll proteins isolated to date have similar molecular weights ranging from 34,500 to 39,00.0 (Tables I and II ).
  • The proteins from a particular species all have the same subunit number, and both monQmeric and dimeric proteins were isolated.

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'
BNL-21729
Peridinin-Chlorophyll
a
Proteins
of
Dinoflagellate
Algae
Harold
W.
Siegelman*,
J.
Helen
Kycia*,
and
Francis
T.
Haxot
*
Biology
Department,
Brookhaven
National
Laboratory,
Upton,
NY
11973
and
tScripps
Institution
of
Oceanography,
University
of
California,
San
Diego,
Callfurnia
92093
,------NOTICE
-
------,
This report
was
prepared as an account
of
wo
rk
sponsored by the United States Government. Neither
the United States nor the United States Energy
R~ar
c
h
and Development Administntion, nor any
of
thett employees, nor any
of
their contracton
subcon
tracton
, or their employees, makes
an;
~r~nty,
upreu
or
implied,
ur
assumes any
legaJ
liability or responsibility for the accuracy, completeness
or
u.teful~e•
of
any information, apparatus, product or
pro~
d~osed,
or represents that its
use
would not
tnfnn&e pnvately owned
rl,hts
.
or
C!.o/JT£/IC!T
No, g (3o -
0-l'
T n
JNLIMIT

DISCLAIMER
This report was prepared as an
account
of
work
sponsored
by
an
agency
of
the United States Government. Neither the United States
Government
nor
any
agency Thereof,
nor
any
of
their
employees,
makes
any
warranty, express
or
implied,
or
assumes
any
legal
liability
or
responsibility
for
the accuracy, completeness,
or
usefulness
of
any
information, apparatus, product,
or
process
disclosed,
or
represents
that
its
use
would
not
infringe
privately
owned rights. Reference herein
to
any
specific
commercial product,
process,
or
service
by
trade name, trademark, manufacturer,
or
otherwise does
not
necessarily
constitute
or
imply
its
endorsement,
recommendation,
or
favoring
by
the United States Government
or
any
agency
thereof. The views and
opinions
of
authors expressed herein
do
not
necessarily state
or
reflect those
of
the United States
Government
or
any
agency
thereof.

DISCLAIMER
Portions
of
this
document
may
be
illegible
in
electronic
image
products.
Images
are
produced
from
the
best
available
original
document.

-2-
INTRODUCTION
The
pigments
which
function
as
the
energy
collection
systems
for
photosynthesis
are
either
tetrapyrroles
or
carotenoids.
In
the
oceans,
which
cov~r
over
70%
of
the
surface
of
the
earth,
carotenoids
may be more
important
than
chlorophylls
for
photosynthetic
energy
capture
by
phytoplankton.
A
characteristic
feature
of
the
principal
marine
phytoplankton
is
the
possession
of
a
high
l:c:t.rotenoid
content.
ln
general
each
major
group
of
phytoplankton
has
a
specific
carotenoid
which
accounts
for
a
major
portion
of
the
total
carotenoid
content.
The
accessory
pigment
function
of
fucoxanthin
and
peridinin
. 6
have
long
been
known ,
and
the
same
function
was
recently
demonstrated
for
19
1
-hexanoyloxyfucoxanthin
with
Coccolithus
huxeyi
clone
BT-6
(F.
T.
Haxo,
unpublished).
The
distribution
of
these
photosynthetically-active
carotenoids
are
as
follows:
Algal
class
Predominant
carotenoid
Dinophyceae
(dinoflagellates)
P
"d"
. 15
er1.
1.n1.n
Bacillariophyceae
(diatoms)
Fucoxanthin
4
Coccolithophoraceae
(coccolithophorids)
Coccolithus
huxleyi
(clone
BT-6)
19
1
-Hexanoyloxyfucoxanthin
1
The
occurrence
of·
19
1
-hexanoyloxyfucoxanthin
in
other
coccolithophorids
has
not
yet
been
eBtablished,
and
fucoxanthin
is
generally
considered
the
dominant
carotenoid
of
the
coccolithophorids.
In
consequence
of
their
carotenoid
pig-
ment
content,
the
marine
phytoplankton
are
yellow-brown
to
yellow-green
in
color.

-3-
These
organisms
all
contain
chlorophylls
a
and
c.
The
spectral
composition
of
the
light
which
penetrates
the
water
column
changes
with
increasing
depth.
The
red
portion
of
the
spectrum
is
at-
tenuated
by
the
red
absorbance
bands
of
water.
The
blue
portion
of
the
visible
spectrum
is
diminished
by
Rayleigh
scattering
and
absorption
by
yellow
pigments.
The
blue-green
to
green
portion
of
the
visible
spectrum
(480-570
nm)
has
maximal
transmission
in
the
water
column,
and
is
the.
region
of
maximal
absorbance
of
many
c·arotenoids.
12
Schutt
first
isolated
peridinin
and
provided
substantial
evidence
for
the
presence
of
soluble
carotenochlorophyll
proteins
in
dinoflagellate
algae
in
1890.
. 2 3
Bode
and
Bode
and
Hastings
found
that
aqueous
extracts
of
(
Gonyaulax
polyedra
were
red
and
that
the
color
was due
to
perdinin
bound
to
protein.
Haidak
et
al?
reported
that
the
red
protein
from
Q.
polyedra
has
a
molecular
weight
of
about
38,000
and
contained
both
peridinin
and
chlorophyll.
ALGAL
CULTURES
Detailed
studies
on
the
perdinin-chlorophyll
~-proteins
were
initiated
at
Brookhaven
National
Laboratory
with
Amphidinium
carterae
(Plymouth
450).
Dr.
Luigi
Provasoli
suggested
the
use
of
carterae
for
these
studies
and
generously
provided
the
culture
and
advice
on
growing
the
alga.
Our
initial
efforts
were
concerned
with
the
development
of
large-scale
culture
techniques
7
to
provide
a
continuous
and
dependable
supply
of
algae
culture
methods
pre-
viously
used
for
large
scale
culture
of
other
microalgae
proves
satisfactory
13
The
alga
was
readily
cultivated
on a
large
scale,
160
liters,.
in
the
ASP
7
arti-
ficial
marine
media
of
Provasoli
11
supplemented
with
a
soil
extract.
A
pure
culture
of
the
alga
was
obtained
by
the
use
of
agar
p.lating
a.nd
antiobiotics.
.;

Citations
More filters
Journal ArticleDOI
TL;DR: Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a, and proposelecular topologies for sPCP consistent with these findings.
Abstract: The water-soluble peridinin--chlorophyll a--proteins (sPCP) from three symbiotic dinoflagellates, Symbiodinium microadriaticum, S. kawagutii and S. pilosum, have been analysed for their quaternary structure (by using immunoblotting techniques) and spectroscopic characteristics (by using absorption and fluorescence spectra). The sPCP from S. kawagutii is comprised exclusively of a monomeric apoprotein of 35 kDa, whereas sPCP from S. pilosum possesses only a dimeric apoprotein with subunits of 15 kDa each. The sPCP from S. microadriaticum simultaneously contains both. Spectroscopically, sPCP from S. kawagutii is very similar to the 35 kDa species in S. microadriaticum; sPCP from S. pilosum is similar to the 15 kDa species from S. microadriaticum. Gaussian deconvolution analyses of absorption and fluorescence emission spectra show that each holoprotein is comprised of two spectrally distinct forms of chlorophyll a. We propose molecular topologies for sPCP consistent with our findings.

54 citations

Journal ArticleDOI
TL;DR: The conformers of peridinin--chorophyll a proteins (PCP), isolated from various strains of the symbiotic dinoflagellate Symbiodinium (= Gymnodinium) microadriaticum and analysed by isoelectric focusing in polyacrylamide gels, exhibited different patterns.
Abstract: The conformers of peridinin--chorophyll a proteins (PCP), isolated from various strains of the symbiotic dinoflagellate Symbiodinium (= Gymnodinium) microadriaticum and analysed by isoelectric focusing in polyacrylamide gels, exhibited different patterns In most instances the same pattern of conformers was found in each strain when freshly isolated from their respective hosts, after culture, and in two instances also after cloning These observations suggest that characteristic patterns of PCP are diagnostic of particular strains of S microadriaticum Evidence is presented that generally the patterns do not change with environment Analysis of PCP could potentially serve as a tool for the identification of strains of S microadriaticum and could also serve as a marker for the empirical analysis of sexual recombination

41 citations

Journal ArticleDOI
TL;DR: Affinity-purified antibodies prepared against the peridinin-chlorophyll a-protein (PCP) complex from the din oflagellate Heterocapsa pygmaea were employed to study the immunological similarity of PCP among 28 dinoflageLLate species, representing eight genera in four families.
Abstract: Affinity-purified antibodies prepared against the peridinin-chlorophyll a-protein (PCP) complex from the dinoflagellate Heterocapsa pygmaea were employed to study the immunological similarity of PCP among 28 dinoflagellate species, representing eight genera in four families. The anti-HpPCP antibodies cross-reacted with the subunits of PCP apoproteins from all dinoflagellates tested, but did not cross-react with pigment proteins from the chrysophyte Cricosphaera carterae, establishing its specificity for dinoflagellate pigment-protein complexes. Among the dinoflagellates, the PCP apoprotein occurs either as a monomer of about 35 kDa or as an apparent homodimer of about 15 kDa. In some instances, both subunit polypeptides are present simultaneously. The occurrence of different quaternary structures of the PCP apoprotein in different algae can serve as a taxonomic tool, when used in conjunction with other characters.

32 citations

Journal ArticleDOI
TL;DR: Peridinin-chlorophyll a-protein (PCP) complexes isolated from three strains of the symbiotic dinoflagellate Symbiodinium microadriaticum Freudenthal have been found to occur in multiple isoelectric forms, but the pattern of isoeLECTric forms of PCP is characteristic of each strain.
Abstract: Peridinin-chlorophyll a -protein (PCP) complexes isolated from three strains of the symbiotic dinoflagellate Symbiodinium microadriaticum Freudenthal have been found to occur in multiple isoelectric forms, but the pattern of isoelectric forms of PCP is characteristic of each strain. Analysis of PCP after growth of the algae from Tridacna maxima, Cassiopeia frondosa, and Rhodactis sancti-thomae at 22, 57 and 157 μmol m -2 s -1 demonstrated that the patterns remained unchanged. Determination of the native molecular mass, quaternary structure and amino acid composition of two isoelectric forms of PCP derived from algae from Anthopleura elegantissima and Rhodactis sancti-thomae showed similar native molecular masses and amino acid composition, but while PCP from the algae from A. elegantissima is dimeric, PCP from algae from R. sancti-thomae is monomeric. The potential use of PCP as a taxonomic tool in dinoflagellate systematics and the evolution of multiple forms of these pigment-protein complexes are discussed.

19 citations


Cites background from "Peridinin-chlorophyll a proteins of..."

  • ...…interspecific differences (Haxo et al. 1976; Prezelin & Haxo 1970; Siegelman et al. 1977; Meeson et al. 1982), and it has been suggested (Siegelman et al. 1977) th a t the distribution of isoelectric forms of PCP may be employed as a potential taxonomic tool in dinoflagellate…...

    [...]

  • ...…of PCP. Similar studies of PCP from free-living dinoflagellates have demonstrated interspecific differences (Haxo et al. 1976; Prezelin & Haxo 1970; Siegelman et al. 1977; Meeson et al. 1982), and it has been suggested (Siegelman et al. 1977) th a t the distribution of isoelectric forms of PCP may…...

    [...]

  • ...Such modification would appear to be species-specific in the free-living dinoflagellates (Haxo et al. 1970; Siegelman et al. 1977) and strain-specific among the species complex designated S. microadriaticum....

    [...]

Journal ArticleDOI
17 Oct 2014-PLOS ONE
TL;DR: All s PCP introns were gained after fusion of ancestral short sPCP genes, which the authors confirm as occurring once in dinoflagellate evolution.
Abstract: Here we document introns in two Symbiodinium clades that were most likely gained following divergence of this genus from other peridinin-containing dinoflagellate lineages. Soluble peridinin-chlorophyll a-proteins (sPCP) occur in short and long forms in different species. Duplication and fusion of short sPCP genes produced long sPCP genes. All short and long sPCP genes characterized to date, including those from free living species and Symbiodinium sp. 203 (clade C/type C2) are intronless. However, we observed that long sPCP genes from two Caribbean Symbiodinium clade B isolates each contained two introns. To test the hypothesis that introns were gained during radiation of clade B, we compared sPCP genomic and cDNA sequences from 13 additional distinct Caribbean and Pacific Symbiodinium clade A, B, and F isolates. Long sPCP genes from all clade B/B1 and B/B19 descendants contain orthologs of both introns. Short sPCP genes from S. pilosum (A/A2) and S. muscatinei (B/B4) plus long sPCP genes from S. microadriaticum (A/A1) and S. kawagutii (F/F1) are intronless. Short sPCP genes of S. microadriaticum have a third unique intron. Symbiodinium clade B long sPCP sequences are useful for assessing divergence among B1 and B19 descendants. Phylogenetic analyses of coding sequences from four dinoflagellate orders indicate that introns were gained independently during radiation of Symbiodinium clades A and B. Long sPCP introns were present in the most recent common ancestor of Symbiodinium clade B core types B1 and B19, which apparently diverged sometime during the Miocene. The clade A short sPCP intron was either gained by S. microadriaticum or possibly by the ancestor of Symbiodinium types A/A1, A3, A4 and A5. The timing of short sPCP intron gain in Symbiodinium clade A is less certain. But, all sPCP introns were gained after fusion of ancestral short sPCP genes, which we confirm as occurring once in dinoflagellate evolution.

2 citations