TY - JOUR

T1 - Indole-3-1actic Acid is a Weak Auxin Analogue but Not an Anti-auxin

AU - Sprunck, Stefanie

AU - Jacobsen, Hans Jörg

AU - Reinard, Thomas

N1 - Funding Information: This work was supported by DFG grants to H.-J.J. and T.R.

PY - 1995/10

Y1 - 1995/10

N2 - Indole-3-lactic acid (ILA) is a naturally occurring indole derivative, preferably detected in soil bacteria and fungi and only in low amounts in plants. T-DNA gene 5 of Agrobacterium tumefaciens was found to be involved in the synthesis of ILA in transformed plant tissues, but the physiologic relevance for ILA production in plants is unclear. The related molecular structure of ILA to the natural auxin indole-3-acetic acid (IAA) makes ILA a good candidate for an auxin analogue. We examined the possible auxin activity of ILA on elongation, proliferation, and differentiation in Pisum sativum L. Results presented in this paper indicate that there are no or only weak effects of ILA toward the activity of auxins when used in the physiologic concentration range. Furthermore, no antagonistic effects of ILA were found. Biochemical analysis using the equilibrium dialysis binding system resulted in no high affinity ILA binding to an enriched protein fraction containing auxin-binding protein (ABP44), whereas 1-naphthaleneacetic acid exhibited high affinity auxin binding.

AB - Indole-3-lactic acid (ILA) is a naturally occurring indole derivative, preferably detected in soil bacteria and fungi and only in low amounts in plants. T-DNA gene 5 of Agrobacterium tumefaciens was found to be involved in the synthesis of ILA in transformed plant tissues, but the physiologic relevance for ILA production in plants is unclear. The related molecular structure of ILA to the natural auxin indole-3-acetic acid (IAA) makes ILA a good candidate for an auxin analogue. We examined the possible auxin activity of ILA on elongation, proliferation, and differentiation in Pisum sativum L. Results presented in this paper indicate that there are no or only weak effects of ILA toward the activity of auxins when used in the physiologic concentration range. Furthermore, no antagonistic effects of ILA were found. Biochemical analysis using the equilibrium dialysis binding system resulted in no high affinity ILA binding to an enriched protein fraction containing auxin-binding protein (ABP44), whereas 1-naphthaleneacetic acid exhibited high affinity auxin binding.

UR - http://www.scopus.com/inward/record.url?scp=0343628154&partnerID=8YFLogxK

U2 - 10.1007/BF00204911

DO - 10.1007/BF00204911

M3 - Article

AN - SCOPUS:0343628154

VL - 14

SP - 191

EP - 197

JO - Journal of plant growth regulation

JF - Journal of plant growth regulation

SN - 0721-7595

IS - 4

ER -