دورية أكاديمية
SecA supports a constant rate of preprotein translocation.
| العنوان: | SecA supports a constant rate of preprotein translocation. |
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| المؤلفون: | Tomkiewicz D; Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Materials Science Centre Plus, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands., Nouwen N, van Leeuwen R, Tans S, Driessen AJ |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 2006 Jun 09; Vol. 281 (23), pp. 15709-13. Date of Electronic Publication: 2006 Apr 06. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Adenosine Triphosphatases/*physiology , Bacterial Proteins/*physiology , Membrane Transport Proteins/*physiology, Adenosine Triphosphate/metabolism ; Hydrolysis ; Kinetics ; Protein Precursors/metabolism ; Protein Transport ; SEC Translocation Channels ; SecA Proteins |
| مستخلص: | In Escherichia coli, secretory proteins (preproteins) are translocated across the cytoplasmic membrane by the Sec system composed of a protein-conducting channel, SecYEG, and an ATP-dependent motor protein, SecA. After binding of the preprotein to SecYEG-bound SecA, cycles of ATP binding and hydrolysis by SecA are thought to drive the stepwise translocation of the preprotein across the membrane. To address how the length of a preprotein substrate affects the SecA-driven translocation process, we constructed derivatives of the precursor of the outer membrane protein A (proOmpA) with 2, 4, 6, and 8 in-tandem repeats of the periplasmic domain. With increasing polypeptide length, an increasing delay in the time before full-length translocation was observed, but the translocation rate expressed as amino acid translocation per minute remained constant. These data indicate that in the ATP-dependent reaction, SecA drives a constant rate of preprotein translocation consistent with a stepping mechanism of translocation. |
| المشرفين على المادة: | 0 (Bacterial Proteins) 0 (Membrane Transport Proteins) 0 (Protein Precursors) 0 (SEC Translocation Channels) 8L70Q75FXE (Adenosine Triphosphate) EC 3.6.1.- (Adenosine Triphosphatases) EC 7.4.2.4 (SecA Proteins) |
| تواريخ الأحداث: | Date Created: 20060408 Date Completed: 20060823 Latest Revision: 20210209 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1074/jbc.M600205200 |
| PMID: | 16601117 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0021-9258 |
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| DOI: | 10.1074/jbc.M600205200 |