نتایج جستجو برای: parallel import

تعداد نتایج: 248110  

Journal: :The Journal of biological chemistry 2002
Suzanne P Cleary Fui-Ching Tan Kerry-Ann Nakrieko Simon J Thompson Philip M Mullineaux Gary P Creissen Erik von Stedingk Elzbieta Glaser Alison G Smith Colin Robinson

Most chloroplast and mitochondrial proteins are synthesized with N-terminal presequences that direct their import into the appropriate organelle. In this report we have analyzed the specificity of standard in vitro assays for import into isolated pea chloroplasts and mitochondria. We find that chloroplast protein import is highly specific because mitochondrial proteins are not imported to any d...

Journal: :The EMBO journal 1998
K Káldi M F Bauer C Sirrenberg W Neupert M Brunner

We analysed the import pathway of Tim23 and of Tim17, components of the mitochondrial import machinery for matrix-targeted preproteins. Tim23 contains two independent import signals. One is located within the first 62 amino acid residues of the hydrophilic domain that, in the assembled protein, is exposed to the intermembrane space. This signal mediates translocation of Tim23 across the outer m...

Journal: :Cell 2010
Geng Wang Hsiao-Wen Chen Yavuz Oktay Jin Zhang Eric L. Allen Geoffrey M. Smith Kelly C. Fan Jason S. Hong Samuel W. French J. Michael McCaffery Robert N. Lightowlers Herbert C. Morse Carla M. Koehler Michael A. Teitell

RNA import into mammalian mitochondria is considered essential for replication, transcription, and translation of the mitochondrial genome but the pathway(s) and factors that control this import are poorly understood. Previously, we localized polynucleotide phosphorylase (PNPASE), a 3' --> 5' exoribonuclease and poly-A polymerase, in the mitochondrial intermembrane space, a location lacking res...

Journal: :The EMBO journal 2010
Yasushi Tamura Miho Iijima Hiromi Sesaki

Ups1p, Ups2p, and Ups3p are three homologous proteins that control phospholipid metabolism in the mitochondrial intermembrane space (IMS). The Ups proteins are atypical IMS proteins in that they lack the two major IMS-targeting signals, bipartite presequences and cysteine motifs. Here, we show that Ups protein import is mediated by another IMS protein, Mdm35p. In vitro import assays show that i...

Journal: :The Journal of Cell Biology 1991
N Michaud D S Goldfarb

Protein import to the nucleus is a signal-mediated process that exhibits saturation kinetics. We investigated whether signal bearing proteins compete with U2 and U6 snRNPs during import. When injected into Xenopus oocytes, saturating concentrations of P(Lys)-BSA, a protein bearing multiple nuclear localization signals from SV40 large T-antigen, reduce the rate of [125I]P(Lys)-BSA and of [125I]n...

Journal: :The EMBO journal 1998
S Jäkel D Görlich

The assembly of eukaryotic ribosomal subunits takes place in the nucleolus and requires nuclear import of ribosomal proteins. We have studied this import in a mammalian system and found that the classical nuclear import pathway using the importin alpha/beta heterodimer apparently plays only a minor role. Instead, at least four importin beta-like transport receptors, namely importin beta itself,...

Journal: :The Journal of Cell Biology 1990
H F Steger T Söllner M Kiebler K A Dietmeier R Pfaller K S Trülzsch M Tropschug W Neupert N Pfanner

We have identified the yeast homologue of Neurospora crassa MOM72, the mitochondrial import receptor for the ADP/ATP carrier (AAC), by functional studies and by cDNA sequencing. Mitochondria of a yeast mutant in which the gene for MOM72 was disrupted were impaired in specific binding and import of AAC. Unexpectedly, we found a residual, yet significant import of AAC into mitochondria lacking MO...

Journal: :Clothing and Textiles Research Journal 2008

Journal: :Journal of Biological Chemistry 2004

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