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Blood, Vol. 96 No. 2 (July 15), 2000:
pp. 747-753
Protein 4.1R binding to eIF3-p44 suggests an interaction between
the cytoskeletal network and the translation apparatus
Chia-Lung Hou,
Chieh-ju C. Tang,
Steve R. Roffler, and
Tang K. Tang
From the Institute of Life Science, National Defense Medical Center,
and the Institute of Biomedical Sciences, Academia Sinica, Taipei,
Taiwan.
Erythroid protein 4.1 (4.1R) is an 80-kd cytoskeletal protein that
stabilizes the membrane-skeletal network structure underlying the lipid
bilayer. Using the carboxyl terminal domain (22/24 kd) of 4.1R as bait
in a yeast 2-hybrid screen, we isolated cDNA clones encoding a
polypeptide of eIF3-p44, which represents a subunit of a eukaryotic
translation initiation factor 3 (eIF3) complex. The eIF3 complex
consists of at least 10 subunits that play an essential role in the
pathway of protein translation initiation. Northern blot analysis
revealed that eIF3-p44 (approximately 1.35 kb) is
constitutively expressed in many tissues. The essential sequence for
this interaction was mapped to the carboxyl-terminus of 4.1R (residues
525-622) and a region (residues 54-321) of eIF3-p44. The direct
association between 4.1R and eIF3-p44 was further confirmed by in vitro
binding assays and coimmunoprecipitation studies. To characterize the
functions of eIF3-p44, we depleted eIF3-p44 from rabbit reticulocyte
lysates either by anti-eIF3-p44 antibody or by GST/4.1R-80 fusion
protein. Our results show that the eIF3-p44 depleted cell-free
translation system was unable to synthesize proteins efficiently. The
direct association between 4.1R and elF3-p44 suggests that 4.1R may act
as an anchor protein that links the cytoskeleton network to the
translation apparatus.
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