ORIGINAL ARTICLE
Tbl3 encodes a WD40 nucleolar protein with regulatory
roles in ribosome biogenesis
Jindong Wang, Schickwann Tsai
Jindong Wang, Schickwann Tsai, Department of Medicine,
University of Utah School of Medicine, Salt Lake City, UT
84132, United States
Author contributions: Wang J designed and constructed vari-
ous expression vectors, performed localization and ribosome
profling, analyzed the data, prepared the fgures and co-wrote
the manuscript; Tsai S designed the project, performed cell
culture experiments, analyzed the data, prepared the fgures and
co-wrote the manuscript.
Supported by In part by a grant from the St. Perres Fund, No.
11-02011
Correspondence to: Schickwann Tsai, MD, PhD, Depart-
ment of Medicine, University of Utah School of Medicine,
5C402, 30 North 1900 East, Salt Lake City, UT 84132,
United States. schickwann.tsai@hsc.utah.edu
Telephone: +1-801-5850495 Fax: +1-801-5850496
Received: October 27, 2013 Revised: February 15, 2014
Accepted: June 18, 2014
Published online: August 6, 2014
Abstract
AIM: To investigate the subcellular localization and the
function of mouse transducin β-like 3 (Tbl3).
METHODS: The coding sequence of mouse Tbl3 was
cloned from the cDNAs of a promyelocyte cell line by
reverse transcription-polymerase chain reaction. Fusion
constructs of Tbl3 and enhanced green fluorescent
protein (EGFP) were transfected into fibroblasts and
examined by fluorescence microscopy to reveal the
subcellular localization of tbl3. To search for nucleolar
targeting sequences, scanning deletions of Tbl3-EGFP
were constructed and transfected into fibroblasts. To
explore the possible function of Tbl3, small hairpin
RNAs (shRNAs) were used to knock down endogenous
Tbl3 in mouse promyelocytes and fbroblasts. The ef-
fects of Tbl3 knockdown on ribosomal RNA (rRNAs)
synthesis or processing were studied by labeling cells
with 5,6-
3
H-uridine followed by a chase with fresh
medium for various periods. Total RNAs were purifed
from treated cells and subjected to gel electrophoresis
and Northern analysis. Ribosome profling by sucrose
gradient centrifugation was used to compare the
amounts of 40S and 60S ribosome subunits as well as
the 80S monosome. The impact of Tbl3 knockdown on
cell growth and proliferation was examined by growth
curves and colony assays.
RESULTS: The largest open reading frame of mouse
Tbl3 encodes a protein of 801 amino acids (AA) with an
apparent molecular weight of 89-90 kilodalton. It con-
tains thirteen WD40 repeats (an ancient protein-protein
interaction motif) and a carboxyl terminus that is highly
homologous to the corresponding region of the yeast
nucleolar protein, utp13. Virtually nothing is known
about the biological function of Tbl3. All cell lines
surveyed expressed Tbl3 and the level of expression
correlated roughly with cell proliferation and/or biosyn-
thetic activity. Using Tbl3-EGFP fusion constructs we
obtained the frst direct evidence that Tbl3 is targeted
to the nucleoli in mammalian cells. However, no previ-
ously described nucleolar targeting sequences were
found in Tbl3, suggesting that the WD40 motif and/or
other topological features are responsible for nucleolar
targeting. Partial knockdown (by 50%-70%) of mouse
Tbl3 by shRNA had no discernable effects on the pro-
cessing of the 47S pre-ribosomal RNA (pre-rRNA) or
the steady-state levels of the mature 28S, 18S and 5.8S
rRNAs but consistently increased the expression level
of the 47S pre-rRNA by two to four folds. The results
of the current study corroborated the previous fnding
that there was no detectable rRNA processing defects
in zebra fish embryos with homozygous deletions of
zebra fsh Tbl3. As ribosome production consumes the
bulk of cellular energy and biosynthetic precursors,
dysregulation of pre-rRNA synthesis can have negative
effects on cell growth, proliferation and differentiation.
Indeed, partial knockdown of Tbl3 in promyelocytes se-
verely impaired their proliferation. The inhibitory effect
of Tbl3 knockdown was also observed in fbroblasts, re-
sulting in an 80% reduction in colony formation. Taken
World Journal of
Hematology WJ
H
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doi:10.5315/wjh.v3.i3.93
World J Hematol 2014 August 6; 3(3): 93-104
ISSN 2218-6204 (online)
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