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A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese

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A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese. / Johnson, Neil A.; Liu, F; Weeks, P. D.; Hentzen, A. E.; Kruse, H. P.; Parker, J. J.; Laursen, Mette; Nissen, Poul; Costa, C. J.; Gatto, Craig.

I: Archives of Biochemistry and Biophysics, Bind 481, Nr. 2, 20.11.2008, s. 157-168.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Johnson, NA, Liu, F, Weeks, PD, Hentzen, AE, Kruse, HP, Parker, JJ, Laursen, M, Nissen, P, Costa, CJ & Gatto, C 2008, 'A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese', Archives of Biochemistry and Biophysics, bind 481, nr. 2, s. 157-168.

APA

Johnson, N. A., Liu, F., Weeks, P. D., Hentzen, A. E., Kruse, H. P., Parker, J. J., ... Gatto, C. (2008). A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese. Archives of Biochemistry and Biophysics, 481(2), 157-168.

CBE

Johnson NA, Liu F, Weeks PD, Hentzen AE, Kruse HP, Parker JJ, Laursen M, Nissen P, Costa CJ, Gatto C. 2008. A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese. Archives of Biochemistry and Biophysics. 481(2):157-168.

MLA

Johnson, Neil A. o.a.. "A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese". Archives of Biochemistry and Biophysics. 2008, 481(2). 157-168.

Vancouver

Johnson NA, Liu F, Weeks PD, Hentzen AE, Kruse HP, Parker JJ o.a. A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese. Archives of Biochemistry and Biophysics. 2008 nov 20;481(2):157-168.

Author

Johnson, Neil A. ; Liu, F ; Weeks, P. D. ; Hentzen, A. E. ; Kruse, H. P. ; Parker, J. J. ; Laursen, Mette ; Nissen, Poul ; Costa, C. J. ; Gatto, Craig. / A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese. I: Archives of Biochemistry and Biophysics. 2008 ; Bind 481, Nr. 2. s. 157-168.

Bibtex

@article{e6ba36a0fba211dd8f9a000ea68e967b,
title = "A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese",
abstract = "Recombinant Ca(2+)-ATPase from tomato (i.e. LCA1 for Lycopersicon esculentum [Since the identification and naming of LCA1, the scientific name for the tomato has been changed to Solanum lycopersicum.] Ca-ATPase) was heterologously expressed in yeast for structure-function characterization. We investigate the differences between plant and animal Ca pumps utilizing comparisons between chicken and rabbit SERCA-type pumps with Arabidopsis (ECA1) and tomato plant (LCA1) Ca(2+)-ATPases. Enzyme function was confirmed by the ability of each Ca(2+)-ATPase to rescue K616 growth on EGTA-containing agar and directly via in vitro ATP hydrolysis. We found LCA1 to be approximately 300-fold less sensitive to thapsigargin than animal SERCAs, whereas ECA1 was thapsigargin-resistant. LCA1 showed typical pharmacological sensitivities to cyclopiazonic acid, vanadate, and eosin, consistent with it being a P(IIA)-type Ca(2+)-ATPase. Possible amino acid changes responsible for the reduced plant thapsigargin-sensitivity are discussed. We found that LCA1 also complemented K616 yeast growth in the presence of Mn(2+), consistent with moving Mn(2+) into the secretory pathway and functionally compensating for the lack of secretory pathway Ca-ATPases (SPCAs) in plants.",
author = "Johnson, {Neil A.} and F Liu and Weeks, {P. D.} and Hentzen, {A. E.} and Kruse, {H. P.} and Parker, {J. J.} and Mette Laursen and Poul Nissen and Costa, {C. J.} and Craig Gatto",
year = "2008",
month = "11",
day = "20",
language = "English",
volume = "481",
pages = "157--168",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press",
number = "2",

}

RIS

TY - JOUR

T1 - A tomato ER-type Ca2+-ATPase, LCA1, has a low thapsigargin-sensitivity and can transport manganese

AU - Johnson, Neil A.

AU - Liu, F

AU - Weeks, P. D.

AU - Hentzen, A. E.

AU - Kruse, H. P.

AU - Parker, J. J.

AU - Laursen, Mette

AU - Nissen, Poul

AU - Costa, C. J.

AU - Gatto, Craig

PY - 2008/11/20

Y1 - 2008/11/20

N2 - Recombinant Ca(2+)-ATPase from tomato (i.e. LCA1 for Lycopersicon esculentum [Since the identification and naming of LCA1, the scientific name for the tomato has been changed to Solanum lycopersicum.] Ca-ATPase) was heterologously expressed in yeast for structure-function characterization. We investigate the differences between plant and animal Ca pumps utilizing comparisons between chicken and rabbit SERCA-type pumps with Arabidopsis (ECA1) and tomato plant (LCA1) Ca(2+)-ATPases. Enzyme function was confirmed by the ability of each Ca(2+)-ATPase to rescue K616 growth on EGTA-containing agar and directly via in vitro ATP hydrolysis. We found LCA1 to be approximately 300-fold less sensitive to thapsigargin than animal SERCAs, whereas ECA1 was thapsigargin-resistant. LCA1 showed typical pharmacological sensitivities to cyclopiazonic acid, vanadate, and eosin, consistent with it being a P(IIA)-type Ca(2+)-ATPase. Possible amino acid changes responsible for the reduced plant thapsigargin-sensitivity are discussed. We found that LCA1 also complemented K616 yeast growth in the presence of Mn(2+), consistent with moving Mn(2+) into the secretory pathway and functionally compensating for the lack of secretory pathway Ca-ATPases (SPCAs) in plants.

AB - Recombinant Ca(2+)-ATPase from tomato (i.e. LCA1 for Lycopersicon esculentum [Since the identification and naming of LCA1, the scientific name for the tomato has been changed to Solanum lycopersicum.] Ca-ATPase) was heterologously expressed in yeast for structure-function characterization. We investigate the differences between plant and animal Ca pumps utilizing comparisons between chicken and rabbit SERCA-type pumps with Arabidopsis (ECA1) and tomato plant (LCA1) Ca(2+)-ATPases. Enzyme function was confirmed by the ability of each Ca(2+)-ATPase to rescue K616 growth on EGTA-containing agar and directly via in vitro ATP hydrolysis. We found LCA1 to be approximately 300-fold less sensitive to thapsigargin than animal SERCAs, whereas ECA1 was thapsigargin-resistant. LCA1 showed typical pharmacological sensitivities to cyclopiazonic acid, vanadate, and eosin, consistent with it being a P(IIA)-type Ca(2+)-ATPase. Possible amino acid changes responsible for the reduced plant thapsigargin-sensitivity are discussed. We found that LCA1 also complemented K616 yeast growth in the presence of Mn(2+), consistent with moving Mn(2+) into the secretory pathway and functionally compensating for the lack of secretory pathway Ca-ATPases (SPCAs) in plants.

M3 - Journal article

VL - 481

SP - 157

EP - 168

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -