Reference "Identification of a rice RNA- and microtubule-binding protein as the multifunctional protein, a peroxisomal enzyme involved in the beta -oxidation of fatty acids"

Reference ID

6549

Title

Identification of a rice RNA- and microtubule-binding protein as the multifunctional protein, a peroxisomal enzyme involved in the beta -oxidation of fatty acids

Source

The Journal of biological chemistry, 2002, vol. 277, pp. 2419-2429

Authors (3)

Chuong-S-D	Mullen-R-T
Muench-D-G

Abstract

The control of subcellular mRNA localization and translation is often mediated
by protein factors that are directly or indirectly associated with the
cytoskeleton. We report the identification and characterization of a rice seed
protein that possesses both RNA and microtubule binding activities. In vitro UV
cross-linking assays indicated that this protein binds to all mRNA sequences
tested, although there was evidence for preferential binding to RNAs that
contained A-C nucleotide sequence motifs. The protein was purified to
homogeneity using a two-step procedure, and amino acid sequencing identified it
as the multifunctional protein (MFP), a peroxisomal enzyme known to possess a
number of activities involved in the beta-oxidation of fatty acids. The
recombinant version of this rice MFP binds to RNA in UV cross-linking and gel
mobility shift experiments, co-sediments specifically with microtubules, and
possesses at least two enzymatic activities involved in peroxisomal fatty acid
beta-oxidation. Taken together these data suggest that MFP has an important role
in mRNA physiology in the cytoplasm, perhaps in regulating the localization or
translation of mRNAs through an interaction with microtubules, in addition to
its peroxisomal function.