1022-7954/05/4102- © 2005 Pleiades Publishing, Inc.
Russian Journal of Genetics, Vol. 41, No. 2, 2005, pp. 97–111. Translated from Genetika, Vol. 41, No. 2, 2005, pp. 149–165.
Original Russian Text Copyright © 2005 by Kurbatova, Dutova, Trotsenko.
THE HISTORY OF THE DISCOVERY
AND MAIN FUNCTIONS OF PEROXISOMES
Intracellular organelles, peroxisomes, occur in vir-
tually all eukaryotic organisms, except parasitic protists
of the genera
Plasmodium, Trichomonas, Giardia
The ﬁrst reports on microbodies, which today are
called peroxisomes, appeared half a century ago. The
was coined in 1966 by de Duve and
colleagues  after biochemical analysis of metabolic
functions of a subclass of microbodies. These authors
have shown that the most part of hydrogen peroxide
produced in cells is degraded in peroxisomes.
The size of peroxisomes ranges from 0.1 to 1
Depending of the cell type, peroxisomes may have a
spherical, tubular, and even cubic shape (Fig. 1) [3, 4].
A one-layer protein–lipid membrane serves as a bound-
ary between the cytosol and the protein matrix. The per-
oxisome functions are essential, for instance, for syn-
thesis of cholesterol and lipids in animals, glycolysis in
trypanosomes, photorespiration in plant leaves and gly-
oxylate metabolism in germinating seeds, primary
metabolism, oxidation, and assimilation of methanol and
primary n-alkane metabolism in yeasts (Table 1) , and
penicillin synthesis in
Some human disorders, including fatal ones, are
caused by defective peroxisome functioning [5–7].
Hence, the role of these functions may be essential.
The number and size of peroxisomes depend on the
type and physiological properties of cells. Recently, the
mechanisms of peroxisome biogenesis, proliferation,
and degradation have been actively studied. Biogenesis
of peroxisomes was shown to be controlled by proteins
of a special class, peroxins, encoded by
Based on using
mutants, signiﬁcant advances
have been made in studying peroxisome biogenesis in
yeasts. The mutants can be selected on substrates
requiring peroxisomes for utilization (methanol for
, oleate for
, and n-alkanes for
). An efﬁcient isolation procedure of
genes is based on complementation analysis of the
mutants by corresponding gene libraries. In the last two
decades, more than 30 functionally different peroxins
have been isolated in yeasts. For most of these proteins,
orthologs in other eukaryotic species were cloned and
sequenced (Table 2) [9–14].
TRANSPORT OF THE PEROXISOMAL PROTEINS
Many of peroxins identiﬁed so far are involved in
matrix protein transport. The corresponding
mutants have “empty” peroxisomes, while their perox-
isomal matrix proteins are localized in the cytosol.
Other mutants, belonging to a minor group (
pex 3, 16,
) are defective at genes involved both in
Structural, Functional and Genetic Aspects
of Peroxisome Biogenesis
E. M. Kurbatova
, T. A. Dutova
, and Yu. A. Trotsenko
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences,
Pushchino, Moscow oblast, 141290 Russia
Fax: (095) 956-33-70; e-mail: email@example.com
Russian State Research Institute for Genetics and Selection of Microorganisms, Moscow, 113545 Russia
Fax: (095) 315-05-01; e-mail: firstname.lastname@example.org
Received April 22, 2004; in ﬁnal form, October 15, 2004
—Intracellular organelles, peroxisomes, occur in cells of most eukaryotic species. Human severe con-
genital disorders are associated with defective assembly and functioning of peroxisomes, which partly explains
the attention of researchers paid to peroxisome biogenesis. It has been shown that peroxisomes are involved in
the realization of eukaryotic developmental programs (in particular, neuroblast differentiation and postembry-
onic development). Cytobiochemical and electron-microscopic studies of peroxisomal mutations showed that
the primary role in peroxisome biogenesis is played by synthesis of speciﬁc proteins (peroxins) and their trans-
port and incorporation into peroxisome membranes. More than 30 peroxin-encoding genes have been exam-
ined. These proteins are synthesized on free polysomes and transported into peroxisomes by means of speciﬁc
signaling peptides, PTS1, PTS2, and PTS3. The import of matrix proteins depends on at least two shuttle recep-
tor proteins, Pex5p and Pex7p. Some proteins regulating peroxisome proliferation in cells have been identiﬁed.