Interacciones

Proteína - Proteína

Fuertes (t = s, min)
Complejos proteicos (estables)

Débiles (t = s, ms)

Complejo intermediario (transitorio)
en una reacción enzimática
Interactions between functional groups

Schwikowski et al.(2000) Nature Biotech. 18, 1257 - 1261

Interactions between proteins of different compartments

Schwikowski et al.(2000) Nature Biotech. 18, 1257 - 1261

 Yeast SH3 domains — which recognize proline-
rich peptides — generated a network containing
394 interactions among 206 proteins

Tong et al. (2002) Science 295, 321-324

An interaction map of the yeast proteome
assembled from published interactions

Schwikowski et al.(2000) Nature Biotech. 18, 1257 - 1261

Protein network in Saccharomyces cerevisiae

..\..\LINKS\Ho Nature(2002).pdf

Ho et al. (2002) Nature 415, 180

 Analysing protein interactions:
Systematic identification of protein
complexes in Saccharomyces
cerevisiae by mass spectrometry

Kumar & Snyder (2002) Nature 415, 123-124

Ho, Y et al. (2002) Nature 415, 180 - 183
How does a trimeric G protein on the inside of a cell membrane
respond to activation by a transmembrane receptor?

Trimeric () G
proteins relay signals
from transmembrane
receptors to
intracellular enzymes
and ion channels,
thereby mediating
vision, smell, taste and
the actions of many
hormones and
neurotransmitters

T. Iiri et al. (1998) Nature 394, 35-38

 The GTPase cycle of trimeric G proteins

The 'turn-on' step begins when

the activated receptor (R*)
associates with the trimer of
(GDP), causing dissociation of
GDP. Then GTP binds to the
complex of R* with the trimer in
its 'empty' state (e), and the
resulting GTP-induced
conformational change causes
GTP to dissociate from R* and
from . After the 'turn-off' step
(hydrolysis of bound GTP to GDP
and inorganic phosphate, Pi), GDP
reassociates with .

T. Iiri et al. (1998) Nature 394, 35-38

 Contacts between G (left) and G-GDP (right)

Red dashed lines indicate contacts that appear to be required for receptor
activation but not for G–G association; green dashed lines indicate
contacts that are important for both functions
T. Iiri et al. (1998) Nature 394, 35-38
How does a trimeric G protein on the inside of a cell membrane
respond to activation by a transmembrane receptor?

Biomedical relevance:
G-protein mutations in
patients with hypertension
and inherited endocrine
disorders enhance or
block signals from
stimulated receptors.

T. Iiri et al. (1998) Nature 394, 35-38

PARP-1: A Perpetrator of
Apoptotic Cell Death

Apoptotic cell death is triggered by

activation of the nuclear enzyme
poly(ADP-ribose) polymerase-1
(PARP-1).

Through unknown mechanisms,

PAR formation and NAD+
depletion may trigger a cascade of
events.

A. Chiarugi & M.A. Moskowitz (2002) Science 297, 200

 Fd
OUT
PS II PS I
e* Q e*

cyt b6-f
h complex h

e Pc (Cu + )
IN e
cyt c6 (Fe2+ )

H 2O

Navarro et al. (1997) J. Biol. Inorg. Chem. 2, 11-22

PSI-driven Electron Transfer

light
b6f
Fd

PS I
Pc Cyt c6
FromCytochrome c6toPlastocyanin

Cyt
I II III
Pc
I II III

Navarro et al. (1997) J. Biol. Inorg. Chem. 2, 11-22

 Oxygen content of the earth's atmosphere
1

Berkner-Marshall Point
(fractions of 21% v/v)

(Terrestrial life)
Atmospheric Level

0.1

Pasteur Point
(O2respiration)
PROKARYOTES
0.01
EUKARYOTES
Photosynthetic
O2 production

0.001
4 3 2 1 0
Time (109 years ago)
(Adapted from Peschek, 1996)
 2-
S
SO42-
Availability
Fe

Cu

4 3 2 1 0
Time (109 years ago)
(Adapted from Williams & Silva, 1997)
Cu ligands:
His-35 Cys-84
His-87 Met-92

Plastocyanin
Heme ligands:
His-19 Met-61

Cytochrome c6
Isoelectric point of cytochrome c6 and plastocyanin
isolated from different organisms
___________________________________________________

Organism Protein pI
___________________________________________________

Spinach Plastocyanin 4.2

Monoraphidium Plastocyanin 3.7

Cytochrome c6 3.6
Anabaena Plastocyanin 9.0
Cytochrome c6 9.0
Synechocystis Plastocyanin 5.5
Cytochrome c6 5.6
____________________________________________________
Cytochrome c6

Plastocyanin

De la Rosa et al. (2002) Bioelectrochemistry 55, 41-45

Photosynthetic
organisms growing
under controlled
conditions
 Spinach PC

200 s Anabaena PC

7 ms
A = 2 x 10-3

Monoraphidium PC
A = 2 x 10-3

200 s

Synechocystis PC

500 s
Monoraphidium Cyt c6

200 s
 KA KR
Protred + PSI red [Protred ... PSIred] [Protred ... PSIred]*
1 2 3
h h h

K'A K'R
Protred + PSIox [Protred ... PSIox ] [Protred ... PSIox ]*
1' 2' 3'
ket

Routes h
a: 1 1' 2' 3' 4
h Protox + PSI red 4
b: 1 2 2'h 3' 4
c: 1 2 3 3' 4

De la Rosa et al. (2002) Bioelectrochemistry 55, 41-45

KINETIC TYPES FOR THE REACTION MECHANISM

Type I

Protred + PSIox  Protox + PSIred

Type II

Protred + PSIox [Protred ... PSIox]  Protox + PSIred

Type III

Protred + PSIox [Protred ... PSIox] [Protred ... PSIox]*  Protox + PSIred

Navarro et al. (1997) J. Biol. Inorg. Chem. 2, 11-22

Flexibilidad estructural de la plastocianina