Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2012 Oct 5;40(22):11583–11593. doi: 10.1093/nar/gks910

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2012. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 2. — A subcomplex of human mtRNase P has tRNA methyltransferase activity. (A) In vitro transcribed (mt)tRNA^Ile labelled by [α-³²P]guanosine triphosphate was incubated with SAM and either HeLa cell mitochondrial extract (mt extract; lane 2), recombinant TRMT10C (lane 3) or mtRNase P reconstituted from its recombinant components (TRMT10C, SDR5C1, PRORP; lane 4). The tRNA hydrolysate was resolved by TLC; origin and direction of migration, and the positions of guanosine monophosphate (G) and its methylated derivatives (m¹G and ) are indicated to the left. (B) (Mt)tRNA^Tyr specifically labelled at the linkage between tRNA-position 8 and 9 only was incubated with HeLa cell mitochondrial extract (lane 4), with the indicated recombinant proteins (lanes 2, 3, 8), with combinations (mixtures) of those (lanes 5–7) or with recombinant TRMT10C and SDR5C1 purified as a complex (lane 9). The tRNA hydrolysate was resolved by TLC; direction of migration and the positions of G and m¹G are indicated to the left; only the informative part of the TLC is shown. (C) (Mt)tRNA^Lys labelled at the linkage between tRNA-position 8 and 9 was incubated with HeLa cell mitochondrial extract (lane 2), with the recombinant TRMT10C–SDR5C1 complex (lane 3) or with TRMT10C and SDR5C1 separately (lanes 4, 5). The tRNA hydrolysate was resolved by TLC; direction of migration and the positions of A and m¹A are indicated to the left; only the informative part of the TLC is shown.

Inline graphic — A subcomplex of human mtRNase P has tRNA methyltransferase activity. (A) In vitro transcribed (mt)tRNA^Ile labelled by [α-³²P]guanosine triphosphate was incubated with SAM and either HeLa cell mitochondrial extract (mt extract; lane 2), recombinant TRMT10C (lane 3) or mtRNase P reconstituted from its recombinant components (TRMT10C, SDR5C1, PRORP; lane 4). The tRNA hydrolysate was resolved by TLC; origin and direction of migration, and the positions of guanosine monophosphate (G) and its methylated derivatives (m¹G and ) are indicated to the left. (B) (Mt)tRNA^Tyr specifically labelled at the linkage between tRNA-position 8 and 9 only was incubated with HeLa cell mitochondrial extract (lane 4), with the indicated recombinant proteins (lanes 2, 3, 8), with combinations (mixtures) of those (lanes 5–7) or with recombinant TRMT10C and SDR5C1 purified as a complex (lane 9). The tRNA hydrolysate was resolved by TLC; direction of migration and the positions of G and m¹G are indicated to the left; only the informative part of the TLC is shown. (C) (Mt)tRNA^Lys labelled at the linkage between tRNA-position 8 and 9 was incubated with HeLa cell mitochondrial extract (lane 2), with the recombinant TRMT10C–SDR5C1 complex (lane 3) or with TRMT10C and SDR5C1 separately (lanes 4, 5). The tRNA hydrolysate was resolved by TLC; direction of migration and the positions of A and m¹A are indicated to the left; only the informative part of the TLC is shown.