The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo.

No abstract is available for this paper.

• Publication year

  1998

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  1998-03-03

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1073/PNAS.95.5.2296PMID 9482879PMCID PMC19325
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The protein encoded by the MFT1 gene is a targeting factor for mitochondrial precursor proteins, and not a core ribosomal protein

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  1996cited by this paper
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  1996cited by this paper
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  1996cited by this paper
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  1996cited by this paper
• Snapshots of membrane-translocating proteins.

  1996cited by this paper
• The intrinsic ability of ribosomes to bind to endoplasmic reticulum membranes is regulated by signal recognition particle and nascent-polypeptide-associated complex.

  1995cited by this paper
• Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum.

  1995cited by this paper
• NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center

  1995cited by this paper
• Reconstitution of the initial steps of mitochondrial protein import

  1995cited by this paper
• An ABC transporter in the mitochondrial inner membrane is required for normal growth of yeast.

  1995cited by this paper
• The protein import receptor of mitochondria.

  1995cited by this paper
• MSF, a novel cytoplasmic chaperone which functions in precursor targeting to mitochondria.

  1994cited by this paper
• A protein complex required for signal-sequence-specific sorting and translocation

  1994cited by this paper
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  1994cited by this paper
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  1994cited by this paper
• Co-translational protein import into mitochondria: an alternative view.

  1993cited by this paper
• GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation

  1993cited by this paper
• The EGD1 product, a yeast homolog of human BTF3, may be involved in GAL4 DNA binding

  1992cited by this paper
• The methionine‐rich domain of the 54 kDa subunit of signal recognition particle is sufficient for the interaction with signal sequences.

  1992cited by this paper
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  1992cited by this paper
• The translation machinery and 70 kd heat shock protein cooperate in protein synthesis.

  1992cited by this paper
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  1992cited by this paper
• Mitochondrial porin can be translocated across both endoplasmic reticulum and mitochondrial membranes.

  1992cited by this paper
• The signal recognition particle in S. cerevisiae.

  1991cited by this paper
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  1989cited by this paper
• The most abundant small cytoplasmic RNA of Saccharomyces cerevisiae has an important function required for normal cell growth

  1989cited by this paper
• Fluorescence microscopy methods for yeast.

  1989cited by this paper
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  1988cited by this paper
• A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

  1988cited by this paper
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  1986cited by this paper
• The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle

  1986cited by this paper
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  1982cited by this paper
• The products of mitochondria-bound cytoplasmic polysomes in yeast.

  1980cited by this paper
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  1975cited by this paper

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