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A plant
PTB-like protein is translocated in the phloem |
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Jeri Brandom 1 , Byung-Chun Yoo
2 , Nien-Chen Huang 1 and William J. Lucas 1 . |
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1 Section of Plant Biology, Division
of Biological Sciences, University of California, Davis, California. 2
Current address: Delaware Biotechnology Institute, Newark, Delaware. |
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There is increasing evidence that plants use non-cell
autonomous movement of ribonucleoproteins (RNPs) to coordinate
regulation of developmental and physiological processes (Haywood et
al. , 2002). Systemic RNA signaling is consistent with the
long-distance transmission of RNA interference and the ability
of translocated aberrant transcripts to alter developmental phenotypes.
In animals, RNA localization is a key determinant of developmental
fate. RNA localization also occurs during embryogenesis and polarized
cell growth in plants (Okita and Choi, 2002). Many RNA-binding
proteins (RBPs) involved in cytoplasmic localization of RNA in
animals have been identified and several of these, by sequence
similarity, have apparent homologs in plants. However, little is
known about proteins that may mediate long-distance RNA signaling
in plants. Polypyrimidine tract-binding protein (PTB, also known
as hnRNP I) is an RBP involved intracellular RNA localization in
animals (Cote et al., 1999). It is a multi-functional RBP with
four loosely conserved RNA-recognition motifs (RRM). PTB binds
to C/U rich polypyrimidine tracts and can be purified from nuclear
extracts with poly(U) affinity chromatography. In addition to RNA-localization,
PTB plays an important role in the intracellular processing of
RNA, including nuclear export of mRNA, alternative splicing of
pre-mRNA, mRNA stabilization, regulation of cap-independent translation,
and poly(A) site cleavage. PTB proteins have been identified in
many animal systems and may be ubiquitous in metazoans. Sequence
similarity indicates the presence of PTB homologs in several plant
species. The Arabidopsis genome contains both PTB homologs
and homologs of proteins that antagonize the activity of PTB in
3′-splice site selection. However, no plant PTB has yet been characterized.
In order to identify components that mediate systemic signaling,
we have conducted a screen of pumpkin phloem exudate for the presence
of poly(U) RNA-binding proteins. We identified a 50-kD phloem localized
protein, Cucurbita maxima RNA-binding protein, 50kD ( CmRBP50 )
with sequence similarity to animal PTBs. Considering the ability
of PTB to mediate RNA localization and influence the ultimate pattern
of gene expression, it is of great interest that there is a PTB-like
protein present in the phloem. Heterograft analysis indicates that
this protein is translocated long-distance in the phloem. Possible
conserved PTB-like activity of CmRBP50, as well as a potential role
for CmRBP50 in selective systemic trafficking of transcripts or long-distance
signaling, is being investigated.
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What are the possible functions of CmRBP50? If CmRBP50 has conserved PTB-like activity, it may play a role in Alternative
splicing of pre-mRNA, poly (A) site cleavage, nuclear export of mRNA,
cytoplasmic localization of mRNA, cap-independent translation, or regulation
of transcription. As an RNA-binding protein that is translocated long
distance in the plant, it may function in long-distance localization
of mRNA. |
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This work is supported by a grant
from the DOE Division of Energy Biosciences (DE-FG03-94ER20134).
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References
Haywood, V., Kragler, F., Lucas, W.J. (2002) Plasmodesmata: pathways
for protein and ribonucleoprotein signaling. Plant
Cell supplement 2002: S303-S325.
Okita, T.W., and Choi, S.-B. (2002) mRNA localization in plants:
targeting to the cell's cortical region and beyond. Curr.
Opin. Plant Biol. 5: 553-559.
Cote, C. A., Gautreau, D., Denegre, J.M., Kress, T.L., Terry, N.A,
Mowry, K.L. (1999) A Xenopus protein related to hnRNP
I has a role in cytoplasmic RNA localization. Mol. Cell. 4: 431-437.
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