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Published 9 December 2002. doi:10.1083/jcb.200203046
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© The Rockefeller University Press, 0021-9525/2002/12/795 $5.00
The Journal of Cell Biology, Volume 159, Number 5, 795-805

Article

 The intranuclear mobility of messenger RNA binding proteins is ATP dependent and temperature sensitive

Alexandre Calapez1,4, Henrique M. Pereira2, Angelo Calado1, José Braga1, José Rino1, Célia Carvalho1, João Paulo Tavanez1, Elmar Wahle3, Agostinho C. Rosa4 and Maria Carmo-Fonseca1

1 Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, 1649-028 Lisboa, Portugal
2 Department of Biological Sciences, Stanford University, Stanford, CA 94305
3 Universität Halle, Institut für Biochemie, 06120 Halle, Germany
4 Instituto de Sistemas e Robótica, Instituto Superior Técnico, 1049-001 Lisboa, Portugal

Address correspondence to Maria Carmo-Fonseca, Instituto de Medicina Molecular, Faculdade de Medicina, Avenida Prof. Egas Moniz, 1649-028 Lisboa, Portugal. Tel.: 351-21-7934340. Fax: 351-21-7951780. E-mail: carmo.fonseca{at}fm.ul.pt

fAter being released from transcription sites, messenger ribonucleoprotein particles (mRNPs) must reach the nuclear pore complexes in order to be translocated to the cytoplasm. Whether the intranuclear movement of mRNPs results largely from Brownian motion or involves molecular motors remains unknown. Here we have used quantitative photobleaching techniques to monitor the intranuclear mobility of protein components of mRNPs tagged with GFP. The results show that the diffusion coefficients of the poly(A)-binding protein II (PABP2) and the export factor TAP are significantly reduced when these proteins are bound to mRNP complexes, as compared with nonbound proteins. The data further show that the mobility of wild-type PABP2 and TAP, but not of a point mutant variant of PABP2 that fails to bind to RNA, is significantly reduced when cells are ATP depleted or incubated at 22°C. Energy depletion has only minor effects on the intranuclear mobility of a 2,000-kD dextran (which corresponds approximately in size to 40S mRNP particles), suggesting that the reduced mobility of PABP2 and TAP is not caused by a general alteration of the nuclear environment. Taken together, the data suggest that the mobility of mRNPs in the living cell nucleus involves a combination of passive diffusion and ATP-dependent processes.

Key Words: mRNA; PABP2; TAP; nucleus; photobleaching


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