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A New Cell Model for Parkinsons Disease 英文参考文献
Open access, freely available online
Research Digest
Synopses of Research Articles
A New Way to Look at
Oxidative Stress
thiol modi?cations in proteins subjected
to varying redox conditions in a living
organism, the bacteria Escherichia coli.
This technique is capable of providing
a global snapshot of the redox state of
protein cysteines during normal and
oxidative stress conditions in the cell.
To detect proteins that have the
ability to undergo stress-induced thiol
modi?cations, Leichert and Jakob
differentially labeled the thiol groups of
thiol-modi?ed and non-thiol-modi?ed
proteins.The proteins were then
separated on two-dimensional gels based
on their charge and molecular weight.
If the technique worked, most thiol-
modi?ed proteins should be detected in
the oxidizing environment of the E. coli
periplasm (the region between the cell’s
membrane layers), and they were.
After proving the method’s ability
to detect proteins whose thiol groups
were oxidized, the next logical step was
to determine what proteins DsbA—the
enzyme that catalyzes disul?de bond
formation in the E. coli periplasm—was
targeting. In E. coli mutant strains that
lack DsbA, Leichert and Jakob identi?ed
a number of proteins with either
many metabolic changes that occur in
oxidatively stressed cells.
Leichert and Jakob’s technique should
be applicable to many different cell
types and organisms and can be used
to investigate the in vivo thiol status of
cellular proteins exposed to virtually any
physiological or pathological condition
that is accompanied by oxidative stress.
The next step will be to investigate just
how thiol modi?cations mediate the
various functions of redox-regulated
proteins.
DOI: 10.1371/journal.pbio.0020374
Chemical reactions lie at the heart
of many biological processes, from
photosynthesis and respiration to cell
signaling and drug metabolism.Thanks
to an atmosphere rich in oxygen, many
organisms use oxygen to carry out these
life processes. But oxygen metabolism
prod
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