DOI: 10.1104/pp.122.3.813. Initial Binding of Preproteins Involving the Toc159 Receptor Can Be Bypassed during Protein Import into Chloroplasts

Initial Binding of Preproteins Involving the Toc159 Receptor Can Be Bypassed during Protein Import into Chloroplasts

10.1104/pp.122.3.813

Crossref journal-article

Oxford University Press (OUP)

Plant Physiology (286)

Abstract

Abstract Two integral outer envelope GTPases, Toc34 and Toc86, are proposed to regulate the recognition and translocation of nuclear-encoded preproteins during the early stages of protein import into chloroplasts. Defining the precise roles of Toc86 and Toc34 has been complicated by the inability to distinguish their GTPase activities. Furthermore, the assignment of Toc86 function is rendered equivocal by recent reports suggesting that the standard protocol for the isolation of chloroplasts results in significant proteolysis of Toc86 (B. Bolter, T. May, J. Soll [1998] FEBS Lett 441: 59–62; G. Schatz [1998] Nature 395: 439–440). We demonstrate that Toc86 corresponds to a native protein of 159 kD in pea (Pisum sativum), designated Toc159. We take advantage of the proteolytic sensitivity of Toc159 to selectively remove its 100-kD cytoplasmic GTPase domain and thereby distinguish its activities from other import components. Proteolysis eliminates detectable binding of preproteins at the chloroplast surface, which is consistent with the proposed role of Toc159 as a receptor component. Remarkably, preprotein translocation across the outer membrane can occur in the absence of the Toc159 cytoplasmic domain, suggesting that binding can be bypassed. Translocation remains sensitive to GTP analogs in the absence of the Toc159 GTP-binding domain, providing evidence that Toc34 plays a key role in the regulation of translocation by GTP.

Bibliography

Chen, K., Chen, X., & Schnell, D. J. (2000). Initial Binding of Preproteins Involving the Toc159 Receptor Can Be Bypassed during Protein Import into Chloroplasts. Plant Physiology, 122(3), 813â822.

Authors 3

Kunhua Chen (first)
Xuejun Chen (additional)
Danny J. Schnell (additional)

References 30 Referenced 98

10.1083/jcb.136.5.983 / J Cell Biol / Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking. by Akita (1997)
10.1016/S0014-5793(98)01525-7 / FEBS Lett / A protein import receptor in pea chloroplasts, Toc86, is only a proteolytic fragment of a larger polypeptide. by Bolter (1998)
10.1016/S0962-8924(99)01554-8 / Trends Cell Biol / Protein import into chloroplasts. by Chen (1999)
10.1146/annurev.cellbio.12.1.1 / Annu Rev Cell Dev Biol / Import and routing of nucleus-encoded chloroplast proteins. by Cline (1996)
10.1104/pp.75.3.675 / Plant Physiol / Thermolysin is a suitable protease for probing the surface of intact pea chloroplasts. by Cline (1984)
10.1016/0003-2697(83)90418-9 / Anal Biochem / A technique for radiolabeling DNA endonuclease fragments to high specific activity. by Feinberg (1983)
10.1104/pp.89.3.993 / Plant Physiol / Chloroplast protein import: quantitative analysis of precursor binding. by Friedman (1989)
10.1083/jcb.129.1.25 / J Cell Biol / Mas37p, a novel receptor subunit for protein import into mitochondria. by Gratzer (1995)
{'key': '2021062510385437200_R9', 'volume-title': 'Antibodies: A Laboratory Manual.', 'author': 'Harlow', 'year': '1988'} / Antibodies: A Laboratory Manual. by Harlow (1988)
10.1016/S0021-9258(18)54172-7 / J Biol Chem / Precursor binding to yeast mitochondria: a general role for the outer membrane protein Mas70p. by Hines (1993)
10.1093/emboj/16.24.7351 / EMBO J / Reconstitution of a chloroplast protein import channel. by Hinnah (1997)
10.1126/science.7801125 / Science / A receptor component of the chloroplast protein translocation machinery. by Hirsch (1994)
10.1016/0076-6879(86)18082-7 / Methods Enzymol / Isolation and characterization of chloroplast envelope membranes. by Keegstra (1986)
10.1126/science.7973656 / Science / Identification of two GTP-binding proteins in the chloroplast protein import machinery. by Kessler (1994)
10.1083/jcb.143.4.991 / J Cell Biol / Tic20 and Tic22 are new components of the protein import apparatus at the chloroplast inner envelope membrane. by Kouranov (1998)
10.1083/jcb.139.7.1677 / J Cell Biol / Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts. by Kouranov (1997)
10.1016/S0021-9258(17)36609-7 / J Biol Chem / Yeast mitochondria lacking the tow import receptors Mas20p and Mas70p can efficiently and specifically import precursor proteins. by Lithgow (1994)
10.1083/jcb.134.2.315 / J Cell Biol / Two components of the chloroplast protein import apparatus, IAP86 and IAP75, interact with the transit sequence during the recognition and translocation of precursor proteins at the outer envelope. by Ma (1996)
{'key': '2021062510385437200_R19', 'volume-title': 'Molecular Cloning: A Laboratory Manual.', 'author': 'Maniatis', 'year': '1982'} / Molecular Cloning: A Laboratory Manual. by Maniatis (1982)
10.1074/jbc.271.39.23846 / J Biol Chem / A protein import receptor of chloroplasts is inserted into the outer envelope membrane by a novel pathway. by Muckel (1996)
10.1093/emboj/16.5.935 / EMBO J / Stable association of chloroplastic precursors with protein-translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone. by Nielsen (1997)
10.1016/S0021-9258(18)48513-4 / J Biol Chem / The binding of precursor proteins to chloroplasts requires nucleoside triphosphates in the intermembrane space. by Olsen (1992)
10.1073/pnas.84.10.3288 / Proc Natl Acad Sci USA / Protein import in chloroplasts requires a chloroplast ATPase. by Pain (1987)
{'key': '2021062510385437200_R24', 'first-page': '93', 'article-title': 'Envelope membrane proteins that interact with chloroplastic precursor proteins.', 'volume': '6', 'author': 'Perry', 'year': '1994', 'journal-title': 'Plant Cell'} / Plant Cell / Envelope membrane proteins that interact with chloroplastic precursor proteins. by Perry (1994)
10.1002/j.1460-2075.1993.tb06095.x / EMBO J / Functional cooperation of mitochondrial protein import receptors in yeast. by Ramage (1993)
10.1038/26620 / Nature / Protein transport: the door to organelles. by Schatz (1998)
10.1016/S0962-8924(97)01111-2 / Trends Cell Biol / A nomenclature for the protein import components of the chloroplast envelope. by Schnell (1997)
10.1126/science.7973649 / Science / Isolation of components of the chloroplast protein import machinery. by Schnell (1994)
10.1046/j.1365-313X.1995.7030401.x / Plant J / A constituent of the chloroplast import complex represents a new type of GTP-binding protein. by Seedorf (1995)
10.1104/pp.121.1.237 / Plant Physiol / GTP promotes the formation of early-import intermediates but is not required during the translocation step of protein import into chloroplasts. by Young (1999)

Dates

Type	When
Created	23 years ago (July 27, 2002, 1:01 a.m.)
Deposited	4 years, 1 month ago (June 25, 2021, 6:45 a.m.)
Indexed	2 weeks, 4 days ago (Aug. 5, 2025, 8:31 a.m.)
Issued	25 years, 5 months ago (March 1, 2000)
Published	25 years, 5 months ago (March 1, 2000)
Published Online	25 years, 5 months ago (March 1, 2000)
Published Print	25 years, 5 months ago (March 1, 2000)

Funders 0

None

BibTeX

@article{Chen_2000, title={Initial Binding of Preproteins Involving the Toc159 Receptor Can Be Bypassed during Protein Import into Chloroplasts}, volume={122}, ISSN={0032-0889}, url={http://dx.doi.org/10.1104/pp.122.3.813}, DOI={10.1104/pp.122.3.813}, number={3}, journal={Plant Physiology}, publisher={Oxford University Press (OUP)}, author={Chen, Kunhua and Chen, Xuejun and Schnell, Danny J.}, year={2000}, month=mar, pages={813–822} }

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  "URL": "http://dx.doi.org/10.1104/pp.122.3.813",
  "relation": {},
  "ISSN": [
    "1532-2548",
    "0032-0889"
  ],
  "subject": [],
  "published-other": {
    "date-parts": [
      [
        2000,
        3,
        1
      ]
    ]
  },
  "published": {
    "date-parts": [
      [
        2000,
        3,
        1
      ]
    ]
  }
}