The surprising complexity of peroxisome biogenesis

被引:72
作者
Olsen, LJ [1 ]
机构
[1] Univ Michigan, Dept Biol, Ann Arbor, MI 48109 USA
关键词
glyoxysomes; peroxisomes; peroxins; protein import; protein targeting;
D O I
10.1023/A:1006092830670
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Peroxisomes are small organelles with a single boundary membrane. All of their matrix proteins are nuclear encoded, synthesized on free ribosomes in the cytosol, and post-translationally transported into the organelle. This may sound familiar, but in fact, peroxisome biogenesis is proving to be surprisingly unique. First, there are several classes of plant peroxisomes, each specialized for a different metabolic function and sequestering specific matrix enzymes. Second, although the mechanisms of peroxisomal protein import are conserved between the classes, multiple pathways of protein targeting and translocation have been defined. At least two different types of targeting signals direct proteins to the peroxisome matrix. The most common peroxisomal targeting signal is a tripeptide limited to the carboxyl terminus of the protein. Some peroxisomal proteins possess an amino-terminal signal which may be cleaved after import. Each targeting signal interacts with a different cytosolic receptor; other cytosolic factors or chaperones may also form a complex with the peroxisomal protein before it docks on the membrane. Peroxisomes have the unusual capacity to import proteins that are fully folded or assembled into oligomers. Although at least 20 proteins (mostly peroxins) are required for peroxisome biogenesis, the role of only a few of these have been determined. Future efforts will be directed towards an understanding of how these proteins interact and contribute to the complex process of protein import into peroxisomes.
引用
收藏
页码:163 / 189
页数:27
相关论文
共 343 条
  • [11] DEVELOPMENT AND APPLICATION OF AN IN-VIVO PLANT PEROXISOME IMPORT SYSTEM
    BANJOKO, A
    TRELEASE, RN
    [J]. PLANT PHYSIOLOGY, 1995, 107 (04) : 1201 - 1208
  • [12] NUCLEIC-ACID (CDNA) AND AMINO-ACID-SEQUENCES OF ISOCITRATE LYASE FROM CASTOR BEAN
    BEECHING, JR
    NORTHCOTE, DH
    [J]. PLANT MOLECULAR BIOLOGY, 1987, 8 (06) : 471 - 475
  • [13] MICROBODIES IN HIGHER-PLANTS
    BEEVERS, H
    [J]. ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1979, 30 : 159 - 193
  • [14] BEHARI R, 1993, J BIOL CHEM, V268, P7315
  • [15] TRANSITION FORM OF MICROBODIES - OVERLAPPING OF 2 SETS OF MARKER PROTEINS DURING THE REARRANGEMENT OF GLYOXYSOMES INTO LEAF PEROXISOMES
    BEHRENDS, W
    BIRKHAN, R
    KINDL, H
    [J]. BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 1990, 371 (01): : 85 - 94
  • [16] PROTON IONOPHORES PREVENT ASSEMBLY OF A PEROXISOMAL PROTEIN
    BELLION, E
    GOODMAN, JM
    [J]. CELL, 1987, 48 (01) : 165 - 173
  • [17] NODULIN-35 - A SUBUNIT OF SPECIFIC URICASE (URICASE-II) INDUCED AND LOCALIZED IN THE UNINFECTED CELLS OF SOYBEAN NODULES
    BERGMANN, H
    PREDDIE, E
    VERMA, DPS
    [J]. EMBO JOURNAL, 1983, 2 (12) : 2333 - 2339
  • [18] STRUCTURE AND METABOLIC CONTROL OF THE YARROWIA-LIPOLYTICA PEROXISOMAL 3-OXOACYL-COA-THIOLASE GENE
    BERNINGER, G
    SCHMIDTCHEN, R
    CASEL, G
    KNORR, A
    RAUTENSTRAUSS, K
    KUNAU, WH
    SCHWEIZER, E
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 216 (02): : 607 - 613
  • [19] A NONMAMMALIAN HOMOLOG OF THE PAF1 GENE (ZELLWEGER-SYNDROME) DISCOVERED AS A GENE INVOLVED IN CARYOGAMY IN THE FUNGUS PODOSPORA-ANSERINA
    BERTEAUXLECELLIER, V
    PICARD, M
    THOMPSONCOFFE, C
    ZICKLER, D
    PANVIERADOUTTE, A
    SIMONET, JM
    [J]. CELL, 1995, 81 (07) : 1043 - 1051
  • [20] BIRKHAN R, 1990, Z NATURFORSCH C, V45, P107