scholarly journals Thylakoid-integrated recombinant Hcf106 participates in the chloroplast twin arginine transport system

Plant Direct ◽  
2018 ◽  
Vol 2 (10) ◽  
pp. e00090 ◽  
Author(s):  
Qianqian Ma ◽  
Kristen Fite ◽  
Christopher Paul New ◽  
Carole Dabney-Smith
Keyword(s):  
Transport System ◽  
Arginine Transport

scholarly journals The Twin Arginine Transport System Appears To Be Essential for Viability in Sinorhizobium meliloti

2010 ◽  
Vol 192 (19) ◽  
pp. 5173-5180 ◽  
Author(s):  
Brad S. Pickering ◽  
Ivan J. Oresnik
Keyword(s):  
Transport System ◽  
Biofilm Formation ◽  
Sinorhizobium Meliloti ◽  
Targeted Mutagenesis ◽  
Cellular Functions ◽  
Unique Data ◽  
Arginine Transport ◽  
Tat Pathway ◽  
Different Types ◽  
Tat System

ABSTRACT The twin arginine transport (Tat) system is responsible for transporting prefolded proteins to the periplasmic space. The Tat pathway has been implicated in many bacterial cellular functions, including motility, biofilm formation, and pathogenesis and symbiosis. Since the annotation of Sinorhizobium meliloti Rm1021 genome suggests that there may be up to 94 putative Tat substrates, we hypothesized that characterizing the twin arginine transport system in this organism might yield unique data that could help in the understanding of twin arginine transport. To initiate this work we attempted a targeted mutagenesis of the tat locus. Despite repeated attempts using a number of different types of media, the attempts at mutation construction were unsuccessful unless the experiment was carried out in a strain that was merodiploid for tatABC. In addition, it was shown that a plasmid carrying tatABC was stable in the absence of antibiotic selection in a tat deletion background. Finally, fluorescence microscopy and live/dead assays of these cultures show a high proportion of dead and irregularly shaped cells, suggesting that the loss of tatABC is inversely correlated with viability. Taken together, the results of this work provide evidence that the twin arginine transport system of S. meliloti appears to be essential for viability under all the conditions that we had tested.

Characterization of l-arginine transport in adrenal cells: effect of ACTH

2006 ◽  
Vol 291 (2) ◽  
pp. E291-E297 ◽  
Author(s):  
Esteban M. Repetto ◽  
Vanesa Pannunzio ◽  
Francisco Astort ◽  
Camila Martinez Calejman ◽  
Marcos Besio Moreno ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Amino Acid ◽  
Transport System ◽  
Zona Fasciculata ◽  
Acid Uptake ◽  
Uptake System ◽  
Amino Acid Transport System ◽  
Cationic Amino Acid ◽  
Arginine Transport

Nitric oxide synthesis depends on the availability of its precursor l-arginine, which could be regulated by the presence of a specific uptake system. In the present report, the characterization of the l-arginine transport system in mouse adrenal Y1 cells was performed. l-arginine transport was mediated by the cationic/neutral amino acid transport system y+L and the cationic amino acid transporter (CAT) y+ in Y1 cells. These Na+-independent transporters were identified by their selectivity for neutral amino acids in both the presence and absence of Na+ and by the effect of N-ethylmaleimide. Transport data correlated to expression of genes encoding for CAT-1, CAT-2, CD-98, and y+LAT-2. A similar expression profile was detected in rat adrenal zona fasciculata. In addition, cationic amino acid uptake in Y1 cells was upregulated by ACTH and/or cAMP with a concomitant increase in nitric oxide (NO) production.

scholarly journals The Bdellovibrio bacteriovorus twin-arginine transport system has roles in predatory and prey-independent growth

Microbiology ◽  
2011 ◽  
Vol 157 (11) ◽  
pp. 3079-3093 ◽  
Author(s):  
Chien-Yi Chang ◽  
Laura Hobley ◽  
Rob Till ◽  
Michael Capeness ◽  
Machi Kanna ◽  
...  
Keyword(s):  
Transport System ◽  
Bacterial Species ◽  
Growth Defect ◽  
Prey Cell ◽  
Arginine Transport ◽  
Rich Media ◽  
Insertional Inactivation ◽  
Sulfur Protein ◽  
Tat System ◽  
Soluble Enzymes

Bdellovibrio bacteriovorus grows in one of two ways: either (i) predatorily [in a host-dependent (HD) manner], when it invades the periplasm of another Gram-negative bacterium, exporting into the prey co-ordinated waves of soluble enzymes using the prey cell contents for growth; or (ii) in a host-independent (HI) manner, when it grows (slowly) axenically in rich media. Periplasmic invasion potentially exposes B. bacteriovorus to extremes of pH and exposes the need to scavenge electron donors from prey electron transport components by synthesis of metalloenzymes. The twin-arginine transport system (Tat) in other bacteria transports folded metalloenzymes and the B. bacteriovorus genome encodes 21 potential Tat-transported substrates and Tat transporter proteins TatA1, TatA2 and TatBC. GFP tagging of the Tat signal peptide from Bd1802, a high-potential iron–sulfur protein (HiPIP), revealed it to be exported into the prey bacterium during predatory growth. Mutagenesis showed that the B. bacteriovorus tatA2 and tatC gene products are essential for both HI and HD growth, despite the fact that they partially complement (in SDS resistance assays) the corresponding mutations in Escherichia coli where neither TatA nor TatC are essential for life. The essentiality of B. bacteriovorus TatA2 was surprising given that the B. bacteriovorus genome encodes a second tatA homologue, tatA1. Transcription of tatA1 was found to be induced upon entry to the bdelloplast, and insertional inactivation of tatA1 showed that it significantly slowed the rates of both HI and HD growth. B. bacteriovorus is one of a few bacterial species that are reliant on a functional Tat system and where deletion of a single tatA1 gene causes a significant growth defect(s), despite the presence of its tatA2 homologue.

scholarly journals Structural model for the protein-translocating element of the twin-arginine transport system

2013 ◽  
Vol 110 (12) ◽  
pp. E1092-E1101 ◽  
Author(s):  
F. Rodriguez ◽  
S. L. Rouse ◽  
C. E. Tait ◽  
J. Harmer ◽  
A. De Riso ◽  
...  
Keyword(s):  
Transport System ◽  
Structural Model ◽  
Arginine Transport

scholarly journals CAT2-mediated l-arginine transport and nitric oxide production in activated macrophages

1999 ◽  
Vol 340 (2) ◽  
pp. 549-553 ◽  
Author(s):  
Donald K. KAKUDA ◽  
Matthew J. SWEET ◽  
Carol L. MACLEOD ◽  
David A. HUME ◽  
Daniel MARKOVICH
Keyword(s):  
Amino Acid ◽  
Transport System ◽  
Transport Systems ◽  
No Production ◽  
Activated Macrophages ◽  
Amino Acid Transport System ◽  
Cationic Amino Acid ◽  
Arginine Transport ◽  
Arginine Uptake ◽  
Expression Studies

Activated macrophages require L-arginine uptake to sustain NO synthesis. Several transport systems could mediate this L-arginine influx. Using competition analysis and gene-expression studies, amino acid transport system y+ was identified as the major carrier responsible for this activity. To identify which of the four known y+ transport-system genes is involved in macrophage-induced L-arginine uptake, we used a hybrid-depletion study in Xenopus oocytes. Cationic amino acid transporter (CAT) 2 antisense oligodeoxyribonucleotides abolished the activated-macrophage-mRNA-induced L-arginine transport. Together with expression studies documenting that CAT2 mRNA and protein levels are elevated with increased L-arginine uptake, our data demonstrate that CAT2 mediates the L-arginine transport that is required for the raised NO production in activated J774 macrophages.

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