Properties of auxin binding sites in different subcellular fractions from maize coleoptiles View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1978-01

AUTHORS

Ulrike Dohrmann, Rainer Hertel, Hiltrud Kowalik

ABSTRACT

In-vitro binding of labeled auxins to sedimentable particles was tested in subcellular fractions from homogenates of maize (Zea mays L.) coleoptiles. The material was fractionated by differential centrifugation or on sucrose density gradients. It was confirmed that the major saturable binding activity (site I) for 1-naphthyl[1-(14)C]acetic acid is associated with vesicles derived from the endoplasmatic reticulum. A second type of specific auxin binding (site II) could be distinguished by several criteria, e.g. by the low affinity towards phenylacetic acid. The particles carrying site II could be clearly separated from markers of the endoplasmatic reticulum, the plasmalemma, the mitochondria and the nuclei, while their density as well as sedimentation velocity correlated with particle-bound acid phosphatase, indicating a localization at the tonoplast. In contrast to site I, binding at site II was hardly affected by a supernatant factor and by sulfhydryl groups. However, the specificity pattern of site II towards auxins and auxin analogs was very similar to that of site I tested in the presence of supernatant factor. The existence of a third auxin receptor localized in plasma membrane-rich gradient fractions was indicated by a preferential in-vitro binding of 2,4-dichlorophenoxyacetic acid. More... »

PAGES

97-106

Journal

TITLE

Planta

ISSUE

2

VOLUME

140

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00384907

DOI

http://dx.doi.org/10.1007/bf00384907

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012286979

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24414464


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