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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 PLoS+One
2015 ; 10
(11
): e0142436
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Mitochondrial Transcription Factor A (TFAM) Binds to RNA Containing 4-Way
Junctions and Mitochondrial tRNA
#MMPMID26545237
Brown TA
; Tkachuk AN
; Clayton DA
PLoS One
2015[]; 10
(11
): e0142436
PMID26545237
show ga
Mitochondrial DNA (mtDNA) is maintained within nucleoprotein complexes known as
nucleoids. These structures are highly condensed by the DNA packaging protein,
mitochondrial Transcription Factor A (TFAM). Nucleoids also include RNA, RNA:DNA
hybrids, and are associated with proteins involved with RNA processing and
mitochondrial ribosome biogenesis. Here we characterize the ability of TFAM to
bind various RNA containing substrates in order to determine their role in TFAM
distribution and function within the nucleoid. We find that TFAM binds to
RNA-containing 4-way junctions but does not bind appreciably to RNA hairpins,
internal loops, or linear RNA:DNA hybrids. Therefore the RNA within nucleoids
largely excludes TFAM, and its distribution is not grossly altered with removal
of RNA. Within the cell, TFAM binds to mitochondrial tRNAs, consistent with our
RNA 4-way junction data. Kinetic binding assays and RNase-insensitive TFAM
distribution indicate that DNA remains the preferred substrate within the
nucleoid. However, TFAM binds to tRNA with nanomolar affinity and these complexes
are not rare. TFAM-immunoprecipitated tRNAs have processed ends, suggesting that
binding is not specific to RNA precursors. The amount of each immunoprecipitated
tRNA is not well correlated with tRNA celluar abundance, indicating unequal TFAM
binding preferences. TFAM-mt-tRNA interaction suggests potentially new functions
for this protein.
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