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Protein binding regions of the mRNAs for the 55 kDa tumor necrosis factor receptor and the glucose transporter 1: sequence homology and competition for cellular proteins
Author(s) -
Kafert Sabine,
Winzen Reinhard,
Loos Anneke,
Bollig Frank,
Resch Klaus,
Holtmann Helmut
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01521-4
Subject(s) - messenger rna , rna binding protein , biology , rna , microbiology and biotechnology , binding protein , glucose transporter , gene expression , sequence motif , gene , biochemistry , insulin , endocrinology
Gene expression is influenced by mechanisms regulating mRNA degradation. Knowledge on regulatory RNA elements involved and on proteins interacting with them is still limited. A 33 nucleotide (nt) region of the 55 kDa tumor necrosis factor receptor (TNFR‐55) mRNA, previously reported by us to engage in such interaction with proteins from U‐937 cells, exhibits homology to a 38 nt regulatory region of the glucose transporter GLUT‐1 mRNA. Labeled RNA fragments comprising these two regions bind similar sets of proteins. Upon phorbol ester‐induced differentiation into macrophage‐like cells, protein binding to both fragments is changed similarly. Furthermore, both compete with each other for protein binding. This suggests that GLUT‐1 and TNFR‐55 RNA share a novel protein binding RNA motif involved in regulation of their half life.