The molecular concept of protein translocation across the outer membrane of chloroplasts

Summary: Chloroplasts, plant organelles which facilitate photosynthesis, originated when photosynthetic bacteria became a part of non-photosynthetic eukaryotic cell. Chloroplast proteins synthetised in the cytosol have to be transported into the organelle, which is facilitated by the Toc complex on...

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Permalink: http://skupni.nsk.hr/Record/nsk.NSK01000716668/Details
Matična publikacija: Croatica chemica acta
81 (2008), 3 ; str. 501-509
Glavni autor: Vojta, Aleksandar (-)
Ostali autori: Fulgosi, Hrvoje (-), Schleiff, Enrico
Vrsta građe: Članak
Jezik: eng
Predmet:
Online pristup: CROATICA CHEMICA ACTA
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100 1 |a Vojta, Aleksandar 
245 1 4 |a The molecular concept of protein translocation across the outer membrane of chloroplasts /  |c Aleksandar Vojta, Hrvoje Fulgosi and Enrico Schleiff. 
300 |b Ilustr. 
504 |a Bibliografija: 77 jed 
504 |a Sažetak 
520 8 |a Summary: Chloroplasts, plant organelles which facilitate photosynthesis, originated when photosynthetic bacteria became a part of non-photosynthetic eukaryotic cell. Chloroplast proteins synthetised in the cytosol have to be transported into the organelle, which is facilitated by the Toc complex on the outer envelope. The preprotein receptors Toc34 and Toc159 associate with the poreforming Toc75 to form the Toc core complex. Toc64 and Toc12 dynamically associate with the core complex and recruit chaperones, forming the intermembrane space complex. Describing Toc159 as integral membrane protein provides insight into its function. After receiving preproteins from Toc34, it uses GTP hydrolysis to push the precursor into the translocation channel. GTP hydrolysis by Toc34 controls its binding/handover cycle. Moreover, different isoforms of Toc components form complexes with different specificity for photosynthetic and non-photosynthetic preproteins. After initial translocation steps, a series of binding spots seems to constitute an affinity chain that guides preproteins further on their translocation pathway. This model parallels the "acid chain" described in mitochondrial import. Considering recent data, a new "big picture" of chloroplast import begins to emerge 
653 0 |a Kloroplasti  |a Proteini  |a Toc kompleks 
700 1 |a Fulgosi, Hrvoje 
700 1 |a Schleiff, Enrico 
773 0 |t Croatica chemica acta  |x 0011-1643  |g 81 (2008), 3 ; str. 501-509  |w nsk.(HR-ZaNSK)000001621 
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856 4 2 |u http://public.carnet.hr/ccacaa/  |y CROATICA CHEMICA ACTA