Translocation and insertion of precursor proteins into isolated outer membranes of mitochondria.

Mayer, Andreas; Lill, Roland; Neupert, Walter

doi:10.1083/jcb.121.6.1233

Cited by 123 publications

(108 citation statements)

References 51 publications

(62 reference statements)

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“…An initial study with outer membrane vesicles demonstrated that they possess a translocation activity on their own. However, translocation into outer membrane vesicles is restricted to those proteins which are integrated into the outer membrane and to a limited set of those proteins which are translocated into the intermembrane space [18]. It should be emphasised that this translocation activity does not require components of the inner membrane, and is restricted to proteins which can be imported into mitochondria in the absence of a membrane potential.…”

Section: The Receptor Complex Of the Outer Membranementioning

confidence: 99%

“…However, according to recent investigations, they can also function independently: (i) isolated outer membrane vesicles possess translocation activity for a subset of proteins [18]; (ii) fusion proteins consisting of a matrix-targeting sequence connected to the enzyme CCHL can be imported into the intermembrane space in the absence of a membrane potential and in a second step, after restoration of the membrane potential, the fusion protein can be imported into the matrix [27].…”

Section: The Import Machinery Of the Inner Membranementioning

confidence: 99%

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Mitochondrial protein import: Mechanisms, components and energetics

Schwarz

Neupert

1994

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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The transport of nuclear-encoded proteins from the cytosol into mitochondria is mediated by targeting (signal) sequences present on precursor forms. Most precursors of the mitochondrial matrix possess amino-terminal signals which characteristically contain hydroxylated and basic amino acids and lack acidic residues. With a minority of precursor proteins, internal sequence motifs can direct proteins to the mitochondria (Planner, N., Hoeben, P., Tropschug, M. and Neupert, W. (1987) J. Biol. Chem. 262, 14851-14854). The presence of a mitochondrial targeting sequence alone, however, is not sufficient for specific targeting to the organeUe and further to the various subcompartments. There is the need for components which recognise the targeting sequences and others which keep the precursor protein in a translocation-competent form. Beyond the recognition step, components are required which mediate transiocation across the mitochondrial membranes. Mitochondria possess two translocation machineries, one in the outer membrane and one in the inner membrane. The matrix space harbors a number of factors which participate in the import of proteins, in their unfolding and folding. Energy is required at several steps of these processes.

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Section: The Receptor Complex Of the Outer Membranementioning

confidence: 99%

Section: The Import Machinery Of the Inner Membranementioning

confidence: 99%

Mitochondrial protein import: Mechanisms, components and energetics

Schwarz

Neupert

1994

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…In addition, the vesicles were able to import the precursor of cytochrome c heme lyase into a protease-protected location (Mayer, Lill & Neupert, 1993). However, insertion of the AAC into these vesicles at the GIP-stage was not observed.…”

Section: The Transport Machineries Of the Inner And Outer Membrane Armentioning

confidence: 93%

Mitochondrial protein import: Specific recognition and membrane translocation of preproteins

et al. 1993

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“…Furthermore, preproteins destined for the matrix only move past the trans-site of the TOM complex if the TIM23 complex comes into play and if a 1Ã across the inner membrane is present ( Fig. 1) (31,67).…”

Section: Translocation Across the Outer Membranementioning

confidence: 99%

Protein Import Into Mitochondria

Paschen¹,

Neupert²

2001

IUBMB Life

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SummaryMost mitochondrial proteins are encoded by the nuclear genome and thus have to be imported into mitochondria from the cytosol. Protein translocation across and into the mitochondrial membranes is a multistep process facilitated by the coordinated action of at least four specialized translocation systems in the outer and inner membranes of mitochondria. The outer membrane contains one general translocase, the TOM complex, whereas three distinct translocases are located in the inner membrane, which facilitates translocation of different classes of preproteins. The TIM23 complex mediates import of matrix-targeted preproteins with Nterminal presequences, whereas hydrophobi c preproteins with internal targeting signals are inserted into the inner membrane via the TIM22 complex. The OXA translocase mediates the insertion of preproteins from the matrix space into the inner membrane. This review focuses on the structural organization and function of the import machinery of the model organisms of Saccharomyces cerevisiae and Neurospora crassa. In addition, the molecular basis of a new human mitochondrial disorder is discussed, the MohrTranebjaerg syndrome. This is the rst known disease, which is caused by an impaired mitochondrial protein import machinery leading to progressive neurodegeneration.

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Translocation and insertion of precursor proteins into isolated outer membranes of mitochondria.

Cited by 123 publications

References 51 publications

Mitochondrial protein import: Mechanisms, components and energetics

Mitochondrial protein import: Mechanisms, components and energetics

Mitochondrial protein import: Specific recognition and membrane translocation of preproteins

Protein Import Into Mitochondria

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