Jr. Han et al., TESTIS BRAIN RNA-BINDING PROTEIN ATTACHES TRANSLATIONALLY REPRESSED AND TRANSPORTED MESSENGER-RNAS TO MICROTUBULES/, Proceedings of the National Academy of Sciences of the United Statesof America, 92(21), 1995, pp. 9550-9554
We have previously identified a testicular phosphoprotein that binds t
o highly conserved sequences (Y and H elements) in the 3' untranslated
regions (UTRs) of testicular mRNAs and suppresses in vitro translatio
n of mRNA constructs that contain these sequences. This protein, testi
s/brain RNA-binding protein (TB-RBP) also is abundant in brain and bin
ds to brain mRNAs whose 3' UTRs contain similar sequences. Here we sho
w that TB-RBP binds specific mRNAs to microtubules (MTs) in vitro, Whe
n TB-RBP is added to MTs reassembled from either crude brain extracts
or from purified tubulin, most of the TB-RBP binds to MTs. The associa
tion of TB-RBP with MTs requires the assembly of MTs and is diminished
by colcemid, cytochalasin D, and high levels of salt; Transcripts fro
m the 3' UTRs of three mRNAs that contain the conserved sequence eleme
nts (transcripts for protamine 2, tau protein, and myelin basic protei
n) are linked by TB-RBP to MTs, whereas transcripts that lack the cons
erved sequences do not bind TB-RBP. We conclude that TB-RBP serves as
an attachment protein for the MT association of specific mRNAs, Consid
ering its ability to arrest translation in vitro, we propose that TB-R
BP functions in the storage and transportation of mRNAs to specific in
tracellular sites where they are translated.