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Transcript
Reconstitution of an Allophycocyanin Trimer Complex Containing
the C-Terminal 2 1 -2 3 kDa Domain of the Core-Membrane
Linker Polypeptide Lcm
L o th a r G o ttsc h a lk 3, Friedrich L ottspeichb and H ugo Scheera
a Botanisches Institut der U niversität, Menzinger Straße 67, D-80638 München,
Bundesrepublik Deutschland
b M ax-Planck-Institut für Biochemie, Am Klopferspitz, D-82152 M artinsried,
Bundesrepublik Deutschland
Z. Naturforsch. 49c, 331-336 (1994); received February 18, 1994
Allophycocyanin, Linker, Anchor Protein, Phycobilisome Core, Mastigocladus laminosus
Allophycocyanin (AP) was isolated from extracts of the cyanobacterium Mastigocladus
laminosus. A fraction enriched in AP-associated polypeptides with apparent molecular masses
of 2 1 -2 3 kD a in SDS-PAGE, was isolated on a preparative scale and identified as a hom olo­
gous mixture of C-terminal fragments o f the core-membrane linker polypeptide Lcm. The com ­
plex (aAPßAP)3-21 - 2 3 kD a was reconstituted and characterized by sucrose density gradient
ultracentrifugation, absorption, fluorescence emission and circular dichroism spectroscopy.
The 2 1 -2 3 kD a polypeptides were found to induce spectral changes in AP similar to those
induced by the small core linker polypeptide Lc8 9. Possible functions of the complex in phycobilisomes are discussed.
Introduction
Phycobilisom es, the light-harvesting an tennae
o f cyanobacteria, red algae and cyanelles, are supram olecular, highly-structured p ro tein com plex­
es located on the thylakoid surface (W ehrm eyer,
1983; G a n tt, 1986). They are com posed o f
chrom opho re-b earin g phycobiliproteins (Scheer,
1982; G lazer, 1985; M acC oll an d G u a rd -F ria r,
1987) abso rb in g light over a wide spectral range,
and o f linker polypeptides which regulate and sta ­
bilize the phycobilisom e structure, b u t also m odify
the lig ht-ab so rp tio n properties o f the phycobili­
proteins (T an d eau de M arsac an d C ohen-B azire,
1977; B ryant, 1991).
Abbreviations: PC, phycocyanin; PEC, phycoerythrocyanin; AP, allophycocyanin; APB, allophycocyanin B; a,
ß, biliprotein subunits; L, linker polypeptide, subscripts
denoting origin and function in phycobilisomes (r, rod;
c, core; rc, rod core; cm, core membrane), superscripts
denoting molecular weight in kDa; OD, optical density;
OD •ml, unit of protein quantity, OD multiplied by sam­
ple volume in ml, subscripts denoting wavelength in nm;
SDS-PAGE, sodium dodecylsulfate-polyacrylamide-gelelectrophoresis; CD, circular dichroism; p/s, peak (^max)to-shoulder (600 nm) absorbance ratio; AA /A m!ix, ratio
of CD signal intensity to absorbance value at >.max.
0 9 3 9 -5 0 7 5 /9 4 /0 5 0 0 -0 3 3 1 $ 0 3.00
© V erlag der Z eitschrift für N atu rfo rsc h u n g ,
D-72072 T übingen
In hem idiscoidal phycobilisom es, an array o f
rods is linked by one or m ore rod-core linker poly­
peptides to the phycobilisom e core. The bi- o r tricylindrical core substructures are form ed by allo­
phycocyanin (A P), tw o m inor biliproteins stru c­
turally related to A P, and the tw o linkers Lc an d
Lcm. The latter, a large polypeptide o f 127 k D a
m olecular m ass in the cyanobacterium M astigo­
cladus laminosus (E steban, 1993), contains several
internal repeats and plays a singular role. It a n ­
chors the core to the m em brane (R edlinger and
G a n tt, 1982; Rusckow ski and Zilinskas, 1982;
R euter and W ehrm eyer, 1990), an d is involved in
the organization o f the core, b u t also carries a
chrom ophore which is p robably the term inal em it­
ter to photosystem II (G indt et al., 1992; Z h ao
et al., 1992).
The key role o f the linker polypeptides in the ag ­
gregate form ation and the fine-tuning o f the a b ­
sorption characteristics o f the phycobiliproteins
has been widely studied, b ut is still only poorly u n ­
derstood. A technique for the isolation o f linker
polypeptides and their fragm ents and for the re­
constitution to biliprotein-linker com plexes re­
cently developed in o u r lab o rato ry (G o ttschalk
et al., 1991 and 1993), has facilitated the study o f
these proteins. H ere, we present results on a com ­
plex o f A P-trim er w ith C -term inal fragm ents o f
the Lcm polypeptide, w hich show s a strong hyper-
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L. G o ttsch alk et al. ■ R e c o n stitu tio n o f an A llophycocyanin T rim er
chrom ism as com p ared to A P-trim ers w ithout
linker. O u r findings m ay be significant in the
present discussion o f the phycobilisom e architec­
ture o f this organism .
Materials and Methods
Absorption and CD m easurem ents were m ade at
an optical density o f 0 .5 -0 .7 5 . Fluorescence em is­
sion was m easured at an optical density o f 0 . 1 at
the a b so rp tio n m axim um in 1 cm cells; excitation
was at 580 nm . Allophycocyanin was isolated from
M astigocladus laminosus on D E 52 (W hatm an),
pre-purified on hydroxy lap atite Bio-Gel H T (BioR ad), an d purified o n F ractogel T SK D E A E 650(2) (M erck) from all co n tam in atio n s o f other
biliproteins an d o f linker polypeptides by the
m ethods previously described (G o ttsch alk et al.,
1991 an d 1993; G o ttsch alk , 1993). 2 1 - 2 3 kD a
polypeptides were isolated w ith buffers containing
3.5 m urea (Serva, p.a. grade) from pre-purified A P
on S-Sepharose F a st Flow (P harm acia) as de­
scribed previously for L c 8 9 (G o ttsch alk et al.,
1993). Reconstitution experim ents - 6 O D 6 2 0 ml
A P (in 230 (j.1 30 m M p otassium p h o sp h ate buffer,
pH 7, con tain in g 3.5 m urea) and 1.2 O D 276-ml en­
riched fractio n o f 2 1 - 2 3 k D a polypeptides (in
400 (j.1 10 m M T ris/H C l, pH 8.9, co ntaining 3.5 m
urea an d 100 m M KC1) were m ixed, reconstituted
in p o tassium p h o sp h ate buffer (700 m M , pH 7.5),
purified by sucrose density g radient u ltracen trifu ­
gation an d characterized by m ethods described
previously fo r com plexes co ntaining L c 8 9 (G ottschalk et al., 1993). T he aggregation state was de­
term ined by 3 - 1 2 % sucrose density gradient
u ltracen trifu g atio n in 700 m M potassium phos­
ph ate buffer (pH 7.5) as described previously
(G o ttsch alk et al., 1993). Am ino acid sequences LysC digestion o f p ro tein bands in polyacrylam ide
m atrix was follow ed by elution and H P L C separa­
tion o f the fragm ents (E ckerskorn and L ottspeich,
1989). N -term inal sequences o f the fragm ents were
determ ined as described previously (E ckerskorn
e ta l., 1988; L ottspeich, 1985). S D S -P A G E was
done according to Läm m li (1970), using a 5%
stacking gel an d a 15% sep aratio n gel.
Results
In a previous p ublication, a new m ethod for the
isolation an d p u rification o f biliproteins and link­
er polypeptides an d for reconstitution o f biliprotein-linker com plexes has been introduced and a p ­
plied to the reconstitution o f (a APß A P ) 3 and of
(a APß A P ) 3 • L c 8 9 (G o ttsch alk et al., 1993). D uring
this w ork, a n o th e r reconstituted com plex,
(a APßAP)3-2 1 -2 3 k D a , had been prepared (G ottschalk et al., 1993), b ut could n ot be further c h a r­
acterized then because the three 2 1 -2 3 k D a poly­
peptides were N -term inally blocked. The related
polypeptides were now enriched by ch ro m a to ­
graphy on S-Sepharose F F . T he fraction o f
2 1 -2 3 k D a polypeptides eluting at ab o u t 100 m M
KC1 was still co n tam in ated by o ther polypeptides
(Fig. 1, lane 1). H ow ever, the m ajo r three bands at
ap p aren t m olecular m asses o f 21 - 23 k D a were the
only ones in this fraction reconstituting stable
com plexes w ith A P (Fig. 1, lane 3), whereas the
contam inations precipitated and were lost during
the reconstitution an d subsequent purification
procedure. T herefore, under circum stances fa­
vouring specific interactions, reconstitution can be
used to obtain pure and specific com plexes from
im pure sam ples. T he polypeptides o f the three
bands form ing a com plex w ith A P were separately
cleaved w ith LysC, and some o f the fragm ents
were sequenced (T able I). All bands contain cleav­
age p roducts identified as fragm ents o f the
C -term inal p a rt o f Lcm, by com parison w ith the
W' V'*
—
-116
—
66
-
45
W 0 _~ 2369
— 24
—
20.1
— 14.2
1
Fig. 1. SDS-PAGE of isolated polypeptides and recon­
stituted complexes. Lane 1: fraction of 21 -2 3 kD a poly­
peptides isolated from S-Sepharose F F column. Lane 2:
(aAPßA P ) 3 complex reconstituted as a control. Lane 3: re­
constituted (aAPßAP)3-21- 2 3 kDa complex. Lane 4: m o­
lecular weight markers (14.2, 20.1, 24, 29, 36, 45, 6 6 and
116 kDa).
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L. G o ttsch alk et al. ■ R eco n stitu tio n o f an A llophycocyanin T rim er
Table I. Sequences of LysC fragments of the upper,
middle and lower band of 21 —23 kD a polypeptides in
the reconstituted complex with AP (Fig. 1, lane 3), and
amino acid positions of identical sequences of Lcm from
Mastigocladus laminosus (Esteban, 1993).
Band
Sequences
Position
upper
L L A D G G LK
AAADLVK
1063-1070
1110-1116
middle
FY TPY PN TK
LL A D G G L K
1029-1037
1063-1070
lower
FY TPY PN TK
LLA D G G L K
A AVEAM VNSP
1029-1037
1063-1070
1071-1080
am ino acid sequence deduced from the D N A se­
quence (E steban, 1993).
E steban (1993) has recently also identified a
23 k D a polypeptide as a C -term inal fragm ent o f
Lcm startin g at am ino acid position 923. The simi­
lar size and sequence overlaps show th a t o u r poly­
peptides are closely related to th e latter. Since they
are N -term inally blocked, it could n o t be d eter­
m ined w hether they differ from each oth er N - or
C -term inally. T he finding o f this fam ily o f closely
related Lcm fragm ents can be rationalized by an
attack o f an endogenous p rotease o r M . laminosus
on regions o f Lcm n o t pro tected inside an A P tri­
m er after subjecting phycobilisom es to dissociat­
ing conditions. 2 1 - 2 3 k D a seems to be a com m on
size for stable fragm ents o f linker polypeptides
protected inside biliprotein trim ers against fu rther
d eg rad atio n (Y u an d G lazer, 1982; Lundell et al.,
1981; Lundell an d G lazer, 1983 a; G o ttsch alk et al.,
1991; G lau ser et al., 1992b); we suggest th a t the
C -term inal d o m ain o f Lcm is follow ing the same
principle.
The basis for the N -term in al block o f o u r iso­
lates is unclear. N -term inally blocked linker poly­
peptides have been rep o rted from o th er organism s
(Lundell et al., 1981; G lauser, 1991; G lauser et al.,
1992 b), b u t are n o t expected for proteolytic frag­
m ents. A block could be due to reaction w ith cyanate ions in the 3.5 m urea solution used th ro u g h ­
o ut the isolation, alth o u g h no such effect has been
observed previously in o u r w ork w ith biliproteins
and linker polypeptides o f M . laminosus isolated
under sim ilar conditio n s (G o ttsch alk et al., 1991
and 1993; G o ttsch alk , 1993).
C om plete co m plexation o f trim eric A P w ith the
2 1 -2 3 k D a polypeptides was ensured by the use o f
an excess o f the latter, as discussed in G o ttsch alk
et al. (1993). T he reconstituted (a APßAP) 3 - 2 1 23 k D a com plex was predom inantly ( > 85% ) tri­
meric; only traces o f m onom eric ( < 8 % ) an d hexameric (< 7% ) aggregates could be detected by
sucrose density gradient u ltracentrifugation. Only
the trim eric fraction from the gradient w as used
for the spectra show n in Fig. 2. N o co n tam in atio n
by APB or the chrom ophore-bearing N -term inus
o f Lcm was detected by spectroscopic m ethods or
SD S-PA G E.
The red ab so rp tio n b an d o f the reconstituted
com plex was at A.max = 651.5 nm , and h ad an ex­
tremely high p/s-ratio o f up to 2.95; the fluores­
cence em ission w as at A.max = 663 nm (Fig. 2 a).
The com plex gave very stro n g C D signals w ith
AA /A max = 4 .7 - 10 ~ 4 (Fig. 2). W hen com pared to
the spectra o f reconstituted (a APß A P ) 3 and
(a APß A P ) 3 • L c 8 9 (G ottschalk et al., 1993), the a b ­
sorption and fluorescence em ission m axim a o f
the new com plex are a t interm ediate values.
X [nm]
Fig. 2. Absorption (A, heavy line, left ordinate), flu­
orescence emission (A, thin line, right ordinate) and CD
spectra (B) o f the reconstituted (aAPßAP)3-21- 2 3 kDa
complex.
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L. G o ttsch alk et al. • R eco n stitu tio n o f an A llophycocyanin T rim er
H ow ever, p/s = 2.95 is the highest value m easured
for any A P-com plex as yet. T he overall shape
and the signal positions o f the C D spectrum are
sim ilar to (a APß A P ) 3 • L c 8 9, but the signal intensities
are ra th e r different. (a APßAP)3-2 1 -2 3 k D a shows
the highest value o f AA / A max for the three com ­
plexes, while the o th er linker-containing com plex,
(a APßAP)3-Lc89, gives the low est am plitudes
(AA / A max = 1 .5 -10“4; G o ttsch alk e t al., 1993). In
(a APßAP)3-2 1 - 2 3 k D a, the negative signal at
a ro u n d 635 nm is m ore p ro n o u n ced th a n th a t at
a ro u n d 594 nm ; in (a APß A P ) 3 • L c 8 9, the intensities
o f these signals are reversed.
Discussion
Lcm is the largest an d m ost com plex linker in
phycobilisom es. It plays a central role in the ener­
gy tran sfer from the rods th ro u g h the core to the
photosystem s. Specific interactio n s w ith the bilip roteins are necessary to explain the functions o f
Lcm as a stru ctu ral protein o f the core, as the a n ­
ch o r protein to the thylakoid m em brane, as a link­
er m odifying the spectral properties o f the asso­
ciated biliproteins, an d as the presum ed term inal
em itter o f the phycobilisom e (R edlinger and
G a n tt, 1982; R usckow ski an d Zilinskas, 1982;
L undell and G lazer, 1983a/b/c; H o u m ard et al.,
1990; C a p u an o e t al., 1991; G in d t e t al., 1992;
Z h ao e t al., 1992). C om plexes co n tain in g Lcm have
been isolated only as large core fragm ents c o n ta in ­
ing also o th er linkers an d biliproteins (Lundell and
G lazer, 1983a/c; Isono an d K a to h , 1987; R euter
and W ehrm eyer, 1990). A P-com plexes containing
a single defined linker have been described only for
L c 8 9 an d rod-core linkers (L undell and G lazer,
1983b; F üglistaller e t al., 1987; G lauser et al.,
1990; G o ttsch alk e t al., 1993).
W e have show n here, th a t the C -term inal d o ­
m ain o f Lcm is capable o f form ing specific com ­
plexes w ith A P trim ers. This d o m ain is n o t singu­
lar in Lcm. Follow ing a N -term inal biliprotein d o ­
m ain, Lcm polypeptides co n tain tw o to four such
repeats, which are also hom ologous to the
N -term inal dom ains o f rod and rod-core linkers
(B ryant, 1988; H o u m ard e t al., 1990). In phycobil­
isomes containing Lcm w ith fo u r repeats, the
C-term inal dom ain has been suggested to link PC
(C apuano et al., 1991) or A P-hexam ers (Isono and
K atoh, 1987; B ryant, 1991) at the basis o f tw o o f
the rods to the core. T his w ould define the C -term inus o f the Lcm o f M . lam inosus an d A n a b a en a sp.
PC C 7120 as a rod-core linker, and w ould have to
be taken into account w ith regard to the proposed
stoichiom etries o f these polypeptides (G lauser
et al., 1992a). R ods w ith A P at their base w ould
either require the interaction o f L r34-5, pc w ith A P,
binding the outer PC -hexam ers to the basal
AP-disc. A lternatively, one o f the presum ed rodcore linkers w ould have to play this role, being in
reality a m isnam ed rod linker. In this context it
is interesting th a t an (a ß )6PC • L r c 2 9 5 •(a ß )3AP • L c 8 9
com plex o f unknow n m o rphology and location
w ithin the phycobilisom e has been isolated and re­
constituted by G lauser et al. (1993). This so-called
rod-core com plex could then also be p a rt o f a spe­
cial rod type.
It should be pointed o ut, how ever, th a t the ex­
perim ental evidence su p p o rtin g this specific phy­
cobilisom e m odel (B ryant et al., 1991; G lauser
et al., 1992a/b; E steban, 1993) is still am biguous.
O ur results are also com patible w ith o th e r models:
the com plex containing the C -term inal dom ain o f
Lcm could be involved in the in teractio n between
neighbouring phycobilisom es, and it could also be
an integral p a rt o f the core.
A cknow ledgem en ts
This w ork was su p p o rted by the D eutsche F o r­
schungsgem einschaft, Bonn (Sonderforschungsbereich 143, project A l) . T he a u th o rs wish to
th an k A. E steban and W. Sidler (E T H Zürich) foi
m aking available im p o rtan t d a ta p rio r to publica
tion.
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