Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Logo for

Science 309 (5731): 140-142

Copyright © 2005 by the American Association for the Advancement of Science

tRNA Actively Shuttles Between the Nucleus and Cytosol in Yeast

Akira Takano,1 Toshiya Endo,1,3,4 Tohru Yoshihisa1,2*

Abstract: Previous evidence suggested that transfer RNAs (tRNAs) cross the nuclear envelope to the cytosol only once after maturing in the nucleus. We now present evidence for nuclear import of tRNAs in yeast. Several export mutants accumulate mature tRNAs in the nucleus even in the absence of transcription. Import requires energy but not the Ran cycle. These results indicate that tRNAs shuttle between the nucleus and cytosol.

1 Department of Chemistry, Graduate School of Science, Japan Science and Technology Corporation, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
2 Research Center for Materials Science, Japan Science and Technology Corporation, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
3 Institute for Advanced Research, Japan Science and Technology Corporation, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
4 Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.

* To whom all correspondence should be addressed. E-mail: tyoshihi{at}

Nuclear-encoded tRNAs are transcribed, processed in the nucleus, and exported to the cytosol to facilitate translation (1). Moreover, a nuclear pool of mature tRNAs also exists. In Saccharomyces cerevisiae, certain mutants defective in nuclear transport and tRNA processing accumulate mature tRNAs in the nucleus, which suggests that nuclear mature tRNAs are intermediates waiting for tRNA export (25). Before export, aminoacyl-tRNA synthetases may monitor their maturation (6). However, we recently found that tRNA-splicing endonuclease localizes to the mitochondrial surface in yeast and that an endonuclease mutant accumulates unspliced pre-tRNAs in the cytosol, which indicates that pre-tRNAs are exported to the cytosol and then spliced (7).

 Fig. 1.. Heterokaryon assay of nuclear import of tRNAs. (A) Heterokaryons formed from MATa cells with sup3+ and MATa cells were incubated in yeast extract, peptone, and dextrose (YPD) for the indicated times and subjected to FISH using probes against mature SptRNA-Meti (mature) and pre-SptRNA-SerUGA (pre). The nucleus and cell outlines are shown in the 4',6'-diamidino-2-phenylindole (DAPI) and Nomarski images, respectively. Target nuclei are marked by arrows. (B) Heterokaryon assays similar to (A) were performed with {Delta}los1 haploids. [View Larger Version of this Image (96K GIF file)]
To understand the origin of nuclear mature tRNAs, we examined whether tRNAs are imported into the nucleus from the cytosol, using heterokaryon assays (8). In S. cerevisiae, a heterokaryon with two different nuclei sharing the same cytosol is formed from karyogamy-deficient MATa and MATa cells. To visualize tRNAs transcribed from one nucleus, a sup3+ gene (SptRNA-SerUGA::SptRNA-Meti) from Schizosaccharomyces pombe was introduced into the MATa strain. sup3+ is transcribed and processed to mature SptRNA-SerUGA and SptRNA-Meti in S. cerevisiae (9). Hetero-karyons between the MATa cells (target) and the MATa cells with sup3+ (donor) were subjected to fluorescence in situ hybridization (FISH). Pre-SptRNA-SerUGA was detected in only one nucleus in a heterokaryon (Fig. 1A, pre, and fig. S2). In a wild-type background for tRNA export, mature SptRNA-Meti was excluded from target nuclei like endogenous tRNAs (Fig. 1A and fig. S4B). {Delta}los1 cells, lacking yeast exportin-t (10, 11), exhibit a moderate defect in nuclear export of mature tRNAs (fig. S4B) (2). In {Delta}los1 heterokaryons, we observed more SptRNA-Meti in target nuclei (Fig. 1B). These data indicate that cytosolic mature tRNAs enter the nucleus.

 Fig. 2.. Treatment with thiolutin causes accumulation of mature tRNA-ProUGG in {Delta}los1 {Delta}msn5 cells. (A) {Delta}los1 {Delta}msn5 cells treated with the indicated concentrations of thiolutin were subjected to Northern hybridization with an anti-pre-tRNA-ProUGG probe. White triangle, primary transcripts; black triangle, end-matured pre-tRNAs. (B) The cells treated with 5 µg/ml thiolutin for the indicated times were subjected to FISH with probes against tRNA-ProUGG and tRNA-TyrGUA. [View Larger Version of this Image (72K GIF file)]
Next, we investigated nuclear import of endogenous tRNAs in cells growing vegetatively. If all nuclear mature tRNAs are newly transcribed, transcription arrest should reduce the nuclear pool of tRNAs through their export. If mature tRNAs are supplied from the cytosol, this should not necessarily be true. A complicating factor is that the signal intensity of mature tRNAs in the wild-type nucleus is lower than that in the cytosol. To circumvent this problem, we used a {Delta}los1 {Delta}msn5 double mutant. Msn5p is a homolog of mammalian exportin-5, which exports the tRNA-eEF1A complex and pre-miRNAs (microRNAs) (1214). {Delta}msn5 by itself did not alter tRNA localization, but the {Delta}los1 {Delta}msn5 mutant showed a strong synthetic defect in mature tRNA export (fig. S4), which suggests that Msn5p contributes to this export. Using this mutant, we analyzed the pool of nuclear tRNAs when transcription was blocked by thiolutin, an RNA polymerase inhibitor (15). In the presence of thiolutin, pre-tRNA-ProUGG disappeared within 1 hour (Northern hybridization, Fig. 2A; FISH, Fig. 2B, pre), whereas mature tRNA-ProUGG and tRNA-TyrGUA accumulated in the nucleus (Fig. 2B, mature). Because no detectable transcription occurred under these conditions, nuclear mature tRNAs must have been supplied from the preexisting cytosolic pool.

To determine whether nuclear import of mature tRNAs requires energy, {Delta}los1 {Delta}msn5 cells were incubated with NaN3 and 2-deoxyglucose (2-dG). Under these conditions, both the primary transcript of tRNA-ProUGG and the gradient of mature tRNA-ProUGG across the nuclear envelope (NE) were no longer detected (Fig. 3A and Fig. 3B, e). Reappearance of the primary transcript 10 min after NaN3 and 2-dG removal indicates rapid replenishment of intracellular adenosine triphosphate (Fig. 3A, –thiolutin). Nuclear accumulation of the mature tRNA was also reestablished after removal of NaN3 and 2-dG, even in the presence of thiolutin (Fig. 3B, h and k). We observed similar results with tRNA-IleAAU encoded by intronless genes (Fig. 3B, i and l). These results indicate that the import of both intron-containing and intronless tRNAs requires energy.

 Fig. 3.. Nuclear import of tRNAs is energy dependent. (A) {Delta}los1 {Delta}msn5 cells grown in YPD (lane 1) were incubated with NaN3 and 2-dG (YPAdG) for 1 hour (lane 2). The cells were chased without (lanes 3 to 8) or with (lanes 9 to 14) thiolutin for the indicated times. Pre-tRNA-ProUGG was detected by Northern hybridization. White triangle, primary transcripts; black triangle, end-matured pre-tRNAs. (B) {Delta}los1 {Delta}msn5 cells were treated as in (A) and were harvested before the energy poison treatment (YPD), after the treatment (YPAdG), and after a 2-hour chase without (–thio.) or with (+thio.) thiolutin. Mature tRNA-ProUGG and tRNA-IleAAU were visualized with FISH. (C) {Delta}los1 {Delta}msn5 cells grown in YPD (lane 1) were incubated in YPAdG (lane 2) and chased with thiolutin for 1 hour (lane 3) or 2 hours (lane 4). Aminoacylation states of tRNA-ProUGG and tRNA-TyrGUA were analyzed with acidic urea-PAGE. Lane 5 contains deacylated tRNA. White and black triangles represent aminoacylated and deacylated tRNAs, respectively. [View Larger Version of this Image (68K GIF file)]

 Fig. 4.. Various tRNA species are imported into the nucleus, and import is Ran independent. (A) cca1-1 cells grown at 23°C were incubated at 37°C for 3 hours, treated with NaN3 and 2-dG for 3 hours at 37°C (YPAdG), and then chased without (–thio.) or with (+thio.) thiolutin for 1.5 hours. Samples were analyzed using FISH (top) and Northern hybridization (bottom) with indicated probes. White, black, and gray triangles represent aminoacylated, deacylated, and 3'-truncated tRNAs, respectively. (B) rna1-1 cells grown at 23°C were incubated at 37°C for 1.5 hours to induce defects and then processed as in (A). [View Larger Version of this Image (73K GIF file)]
We analyzed aminoacylation states of mature tRNAs imported into the nucleus using acidic urea–polyacrylamide gel electrophoresis (urea-PAGE). Mature tRNA-ProUGG and tRNA-TyrGUA in {Delta}los1 {Delta}msn5 cells were present primarily as slower migrating forms even after the chase with thiolutin (Fig. 3C, lanes 1, 3, and 4). These forms were converted to faster migrating forms by base treatment (lane 5), which indicates that the slower migrating tRNAs are aminoacylated. Therefore, imported tRNAs exist mainly in aminoacylated forms in the nucleus.

We asked whether 3'-truncated tRNAs are imported. cca1-1 cells are deficient in both de novo formation and repair of 3'-terminal CCA ends of tRNAs (16), and also in tRNA export (4). We therefore treated cca1-1 cells with NaN3 and 2-dG at a restrictive temperature to abolish the mature tRNA gradient across the NE and chased them with thiolutin. tRNA-TyrGUA and tRNA-IleAAU reaccumulated in the nucleus to similar levels (Fig. 4A, q to t), although the proportions of the 3'-truncated forms of these tRNAs were different (Fig. 4A, bottom). Taken together with the fact that tRNAs in {Delta}los1 {Delta}msn5 cells were full-length tRNAs, these results indicate that various forms of tRNAs are imported.

To determine the contribution of Ran guanosine triphosphatase (GTPase) (17), we examined tRNA import in rna1-1 cells defective in RanGAP (Ran GTPase activating protein). The rna1-1 cells accumulated mature tRNA-TyrGUA in the nucleus at 37°C (2), and this tRNA gradient disappeared upon treatment with NaN3 and 2-dG (Fig. 4B, 37°C, YPAdG). When the cells were transferred to medium with thiolutin, mature tRNA-TyrGUA was reaccumulated (Fig. 4B, +thio.). Because protein import ceased at 37°C in rna1-1 cells (fig. S5), these results suggest that tRNA import is Ran independent.

Our results indicate that nuclear mature tRNAs are supplied from the cytosol and that tRNAs shuttle between these two compartments. Shuttling may contribute to tRNA quality control, because tRNAs have long lifetimes and may run the risk of inappropriate modifications (18). A quality-control system in the nucleus may repair or filter out inactive tRNAs from those shuttling through the nucleus and provide only active tRNAs back to the cytosol. Another controversial possibility would be to supply tRNAs for nuclear translation (19).

References and Notes Back to Top

  1. 1"> A. K. Hopper, E. M. Phizicky, Genes Dev. 17, 162 (2003).[Free Full Text]
  2. 2"> S. Sarkar, A. K. Hopper, Mol. Biol. Cell 9, 3041 (1998).[Abstract/Free Full Text]
  3. H. Grosshans, E. Hurt, G. Simos, Genes Dev. 14, 830 (2000).[Abstract/Free Full Text]
  4. 4"> W. Feng, A. K. Hopper, Proc. Natl. Acad. Sci. U.S.A. 99, 5412 (2002).[Abstract/Free Full Text]
  5. 5"> S. Sarkar, A. K. Azad, A. K. Hopper, Proc. Natl. Acad. Sci. U.S.A. 96, 14366 (1999).[Abstract/Free Full Text]
  6. 6"> E. Lund, J. E. Dahlberg, Science 282, 2082 (1998).[Abstract/Free Full Text]
  7. 7"> T. Yoshihisa, K. Yunoki-Esaki, C. Ohshima, N. Tanaka, T. Endo, Mol. Biol. Cell 14, 3266 (2003).[Abstract/Free Full Text]
  8. 8"> R. Azpiroz, R. A. Butow, Mol. Biol. Cell 4, 21 (1993).[Abstract]
  9. 9"> I. Willis et al., EMBO J. 3, 1573 (1984). [Web of Science][Medline]
  10. 10"> K. Hellmuth et al., Mol. Cell. Biol. 18, 6374 (1998).[Abstract/Free Full Text]
  11. 11"> G.-J. Arts, S. Kuersten, P. Romby, B. Ehresmann, I. W. Mattaj, EMBO J. 17, 7430 (1998).[CrossRef] [Web of Science][Medline]
  12. 12"> A. Kaffman, N. M. Rank, E. M. O'Neill, L. S. Huang, E. K. O'Shea, Nature 396, 482 (1998).[CrossRef][Medline]
  13. M. T. Bohnsack et al., EMBO J. 21, 6205 (2002).[CrossRef] [Web of Science][Medline]
  14. 14"> E. Lund, S. Güttinger, A. Calado, J. E. Dahlberg, U. Kutay, Science 303, 95 (2004).[Abstract/Free Full Text]
  15. 15"> T. Kadowaki et al., J. Cell Biol. 126, 649 (1994).[Abstract/Free Full Text]
  16. 16"> C. L. Wolfe, A. K. Hopper, N. C. Martin, J. Biol. Chem. 271, 4679 (1996).[Abstract/Free Full Text]
  17. 17"> D. Görlich, U. Kutay, Annu. Rev. Cell Dev. Biol. 15, 607 (1999).[CrossRef] [Web of Science][Medline]
  18. 18"> S. Kadaba et al., Genes Dev. 18, 1227 (2004).[Abstract/Free Full Text]
  19. 19"> F. J. Iborra, D. A. Jackson, P. R. Cook, Science 293, 1139 (2001).[Abstract/Free Full Text]
  20. We thank A. K. Hopper, K. Weis, P. A. Silver, Y. Ohya, and J. L. Brodsky for experimental materials and critical reading of our manuscript. We appreciate support from our lab members, especially T. Makio and S. Nishikawa. This work was supported by grants-in-aid for Scientific Research from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.

Supporting Online Material

Materials and Methods

SOM Text

Figs. S1 to S6

Tables S1 to S3


Received for publication 8 April 2005. Accepted for publication 9 May 2005.

Protein Kinase A Is Part of a Mechanism That Regulates Nuclear Reimport of the Nuclear tRNA Export Receptors Los1p and Msn5p.
J. B. Pierce, G. van der Merwe, and D. Mangroo (2014)
Eukaryot. Cell 13, 209-230
   Abstract »    Full Text »    PDF »
tRNA 3' processing in yeast involves tRNase Z, Rex1, and Rrp6.
E. Skowronek, P. Grzechnik, B. Spath, A. Marchfelder, and J. Kufel (2014)
RNA 20, 115-130
   Abstract »    Full Text »    PDF »
Retrograde transfer RNA nuclear import provides a new level of tRNA quality control in Saccharomyces cerevisiae.
E. B. Kramer and A. K. Hopper (2013)
PNAS 110, 21042-21047
   Abstract »    Full Text »    PDF »
Genome-Wide Investigation of the Role of the tRNA Nuclear-Cytoplasmic Trafficking Pathway in Regulation of the Yeast Saccharomyces cerevisiae Transcriptome and Proteome.
H.-Y. Chu and A. K. Hopper (2013)
Mol. Cell. Biol. 33, 4241-4254
   Abstract »    Full Text »    PDF »
Transfer RNA Post-Transcriptional Processing, Turnover, and Subcellular Dynamics in the Yeast Saccharomyces cerevisiae.
A. K. Hopper (2013)
Genetics 194, 43-67
   Abstract »    Full Text »    PDF »
Crystal structure of Cex1p reveals the mechanism of tRNA trafficking between nucleus and cytoplasm.
K. Nozawa, R. Ishitani, T. Yoshihisa, M. Sato, F. Arisaka, S. Kanamaru, N. Dohmae, D. Mangroo, B. Senger, H. D. Becker, et al. (2013)
Nucleic Acids Res. 41, 3901-3914
   Abstract »    Full Text »    PDF »
tRNAHis 5-methylcytidine levels increase in response to several growth arrest conditions in Saccharomyces cerevisiae.
M. A. Preston, S. D'Silva, Y. Kon, and E. M. Phizicky (2013)
RNA 19, 243-256
   Abstract »    Full Text »    PDF »
Retrograde nuclear import of tRNA precursors is required for modified base biogenesis in yeast.
T. Ohira and T. Suzuki (2011)
PNAS 108, 10502-10507
   Abstract »    Full Text »    PDF »
P-body components, Dhh1 and Pat1, are involved in tRNA nuclear-cytoplasmic dynamics.
R. L. Hurto and A. K. Hopper (2011)
RNA 17, 912-924
   Abstract »    Full Text »    PDF »
Nutrient stress does not cause retrograde transport of cytoplasmic tRNA to the nucleus in evolutionarily diverse organisms.
S. C. Chafe, J. B. Pierce, M. B. K. Eswara, A. T. McGuire, and D. Mangroo (2011)
Mol. Biol. Cell 22, 1091-1103
   Abstract »    Full Text »    PDF »
tRNA biology charges to the front.
E. M. Phizicky and A. K. Hopper (2010)
Genes & Dev. 24, 1832-1860
   Abstract »    Full Text »    PDF »
Scyl1 Facilitates Nuclear tRNA Export in Mammalian Cells by Acting at the Nuclear Pore Complex.
S. C. Chafe and D. Mangroo (2010)
Mol. Biol. Cell 21, 2483-2499
   Abstract »    Full Text »    PDF »
Regulation of tRNA Bidirectional Nuclear-Cytoplasmic Trafficking in Saccharomyces cerevisiae.
A. Murthi, H. H. Shaheen, H.-Y. Huang, M. A. Preston, T.-P. Lai, E. M. Phizicky, and A. K. Hopper (2010)
Mol. Biol. Cell 21, 639-649
   Abstract »    Full Text »    PDF »
Utp9p Facilitates Msn5p-mediated Nuclear Reexport of Retrograded tRNAs in Saccharomyces cerevisiae.
M. B.K. Eswara, A. T. McGuire, J. B. Pierce, and D. Mangroo (2009)
Mol. Biol. Cell 20, 5007-5025
   Abstract »    Full Text »    PDF »
MicroRNAs with a nucleolar location.
J. C. Ritland Politz, E. M. Hogan, and T. Pederson (2009)
RNA 15, 1705-1715
   Abstract »    Full Text »    PDF »
A Targeted Bypass Screen Identifies Ynl187p, Prp42p, Snu71p, and Cbp80p for Stable U1 snRNP/Pre-mRNA Interaction.
R. Hage, L. Tung, H. Du, L. Stands, M. Rosbash, and T.-H. Chang (2009)
Mol. Cell. Biol. 29, 3941-3952
   Abstract »    Full Text »    PDF »
Colicin E5 Ribonuclease Domain Cleaves Saccharomyces cerevisiae tRNAs Leading to Impairment of the Cell Growth.
T. Ogawa, M. Hidaka, K. Kohno, and H. Masaki (2009)
J. Biochem. 145, 461-466
   Abstract »    Full Text »    PDF »
Stress-induced tRNA-derived RNAs: a novel class of small RNAs in the primitive eukaryote Giardia lamblia.
Y. Li, J. Luo, H. Zhou, J.-Y. Liao, L.-M. Ma, Y.-Q. Chen, and L.-H. Qu (2008)
Nucleic Acids Res. 36, 6048-6055
   Abstract »    Full Text »    PDF »
Degradation of several hypomodified mature tRNA species in Saccharomyces cerevisiae is mediated by Met22 and the 5'-3' exonucleases Rat1 and Xrn1.
I. Chernyakov, J. M. Whipple, L. Kotelawala, E. J. Grayhack, and E. M. Phizicky (2008)
Genes & Dev. 22, 1369-1380
   Abstract »    Full Text »    PDF »
Utp8p Is a Nucleolar tRNA-binding Protein That Forms a Complex with Components of the Nuclear tRNA Export Machinery in Saccharomyces cerevisiae.
B. R. Strub, M. B.K. Eswara, J. B. Pierce, and D. Mangroo (2007)
Mol. Biol. Cell 18, 3845-3859
   Abstract »    Full Text »    PDF »
Reversibility in nucleocytoplasmic transport.
R. B. Kopito and M. Elbaum (2007)
PNAS 104, 12743-12748
   Abstract »    Full Text »    PDF »
Rapid and Reversible Nuclear Accumulation of Cytoplasmic tRNA in Response to Nutrient Availability.
M. L. Whitney, R. L. Hurto, H. H. Shaheen, and A. K. Hopper (2007)
Mol. Biol. Cell 18, 2678-2686
   Abstract »    Full Text »    PDF »
The ins and outs of tRNA transport.
M. Mirande (2007)
EMBO Rep. 8, 547-549
   Full Text »    PDF »
Inorganic Phosphate Deprivation Causes tRNA Nuclear Accumulation via Retrograde Transport in Saccharomyces cerevisiae.
R. L. Hurto, A. H. Y. Tong, C. Boone, and A. K. Hopper (2007)
Genetics 176, 841-852
   Abstract »    Full Text »    PDF »
Retrograde nuclear accumulation of cytoplasmic tRNA in rat hepatoma cells in response to amino acid deprivation.
H. H. Shaheen, R. L. Horetsky, S. R. Kimball, A. Murthi, L. S. Jefferson, and A. K. Hopper (2007)
PNAS 104, 8845-8850
   Abstract »    Full Text »    PDF »
Conservation of a Masked Nuclear Export Activity of La Proteins and Its Effects on tRNA Maturation.
M. A. Bayfield, T. E. Kaiser, R. V. Intine, and R. J. Maraia (2007)
Mol. Cell. Biol. 27, 3303-3312
   Abstract »    Full Text »    PDF »
Thio Modification of Yeast Cytosolic tRNA Is an Iron-Sulfur Protein-Dependent Pathway.
Y. Nakai, M. Nakai, R. Lill, T. Suzuki, and H. Hayashi (2007)
Mol. Cell. Biol. 27, 2841-2847
   Abstract »    Full Text »    PDF »
The Lsm2-8 complex determines nuclear localization of the spliceosomal U6 snRNA.
M. P. Spiller, K.-L. Boon, M. A. M. Reijns, and J. D. Beggs (2007)
Nucleic Acids Res. 35, 923-929
   Abstract »    Full Text »    PDF »
Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery.
A. T. McGuire and D. Mangroo (2007)
EMBO J. 26, 288-300
   Abstract »    Full Text »    PDF »
Exportin-5 orthologues are functionally divergent among species.
S. Shibata, M. Sasaki, T. Miki, A. Shimamoto, Y. Furuichi, J. Katahira, and Y. Yoneda (2006)
Nucleic Acids Res. 34, 4711-4721
   Abstract »    Full Text »    PDF »
Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA.
A. Noma, Y. Kirino, Y. Ikeuchi, and T. Suzuki (2006)
EMBO J. 25, 2142-2154
   Abstract »    Full Text »    PDF »
The La protein functions redundantly with tRNA modification enzymes to ensure tRNA structural stability..
RNA 12, 644-654
   Abstract »    Full Text »    PDF »
Proteomic Analysis of the Yeast Mitochondrial Outer Membrane Reveals Accumulation of a Subclass of Preproteins.
R. P. Zahedi, A. Sickmann, A. M. Boehm, C. Winkler, N. Zufall, B. Schonfisch, B. Guiard, N. Pfanner, and C. Meisinger (2006)
Mol. Biol. Cell 17, 1436-1450
   Abstract »    Full Text »    PDF »
Rsp5 ubiquitin ligase modulates translation accuracy in yeast Saccharomyces cerevisiae.
RNA 11, 1710-1718
   Abstract »    Full Text »    PDF »
Depletion of Saccharomyces cerevisiae tRNAHis Guanylyltransferase Thg1p Leads to Uncharged tRNAHis with Additional m5C.
W. Gu, R. L. Hurto, A. K. Hopper, E. J. Grayhack, and E. M. Phizicky (2005)
Mol. Cell. Biol. 25, 8191-8201
   Abstract »    Full Text »    PDF »
Retrograde tRNAs.
R. S. Tuma (2005)
J. Cell Biol. 170, 512
   Full Text »    PDF »
Have tRNA, will travel.
E. M. Phizicky (2005)
PNAS 102, 11127-11128
   Full Text »    PDF »
Retrograde movement of tRNAs from the cytoplasm to the nucleus in Saccharomyces cerevisiae.
H. H. Shaheen and A. K. Hopper (2005)
PNAS 102, 11290-11295
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882