TY - JOUR

T1 - Assignment of the Auxin Binding Abilities of ABP44 in Gel

AU - Reinard, Thomas

AU - Achmus, Heike

AU - Walther, Antje

AU - Rescher, Ursula

AU - Klämbt, Dieter

AU - Jacobsen, Hans Jörg

N1 - Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft to T.R. (Re 1012/3-2). We thank Dr. Alan Jones, University of North Carolina at Chapel Hill, for providing the 5-azido-[7-3H]IAA and Dr. Richard Napier, Horticulture Research International, East Mailing, Kent, U.K. We thank Neera Tewari for practical help in the preparation of the manuscript.

PY - 1998/8/1

Y1 - 1998/8/1

N2 - Several approaches were successfully performed to directly assign and characterize auxin binding of ABP44 in gel. The 44 kDa high affinity auxin binding protein ABP44 from pea was tested for its ability to bind 5-azido-[7-3H]-IAA in photoaffinity labeling experiments. Competition experiments with several auxin analogues confirm data published previously (Reinard and Jacobsen 1995). Critical reflections of the limitations of 'the method are also discussed. Immunostaining using the antibody D16 (Napier and Venis 1992), which is directed against the putative binding site of ABP1, revealed that ABP44's auxin binding site is at least partially related to the corresponding site of ABP1. Nevertheless, both proteins do not share any further immunological relationships. Our results with D16 recommend a careful reconsideration of data published by other authors. Furthermore, a 80 kDa, dimeric glutathione dependent formaldehyde dehydrogenase (FDH) from mung bean, described recently, was found to be different from ABP44. In contrast to the described FDH, ABP44 exhibited no FDH activity.

AB - Several approaches were successfully performed to directly assign and characterize auxin binding of ABP44 in gel. The 44 kDa high affinity auxin binding protein ABP44 from pea was tested for its ability to bind 5-azido-[7-3H]-IAA in photoaffinity labeling experiments. Competition experiments with several auxin analogues confirm data published previously (Reinard and Jacobsen 1995). Critical reflections of the limitations of 'the method are also discussed. Immunostaining using the antibody D16 (Napier and Venis 1992), which is directed against the putative binding site of ABP1, revealed that ABP44's auxin binding site is at least partially related to the corresponding site of ABP1. Nevertheless, both proteins do not share any further immunological relationships. Our results with D16 recommend a careful reconsideration of data published by other authors. Furthermore, a 80 kDa, dimeric glutathione dependent formaldehyde dehydrogenase (FDH) from mung bean, described recently, was found to be different from ABP44. In contrast to the described FDH, ABP44 exhibited no FDH activity.

KW - Auxin binding protein

KW - Formaldehyde dehydrogenase

KW - Photoaffinity labeling

KW - Pisum sativum

UR - http://www.scopus.com/inward/record.url?scp=0032143586&partnerID=8YFLogxK

U2 - 10.1093/oxfordjournals.pcp.a029447

DO - 10.1093/oxfordjournals.pcp.a029447

M3 - Article

C2 - 9787462

AN - SCOPUS:0032143586

VL - 39

SP - 874

EP - 878

JO - Plant and Cell Physiology

JF - Plant and Cell Physiology

SN - 0032-0781

IS - 8

ER -