Downregulation of the essential Trypanosoma brucei La protein affects accumulation of elongator methionyl-tRNA
Downregulation of the essential Trypanosoma brucei La protein affects accumulation of elongator methionyl-tRNA
复制标题
DOI:
10.1016/j.molbiopara.2005.06.006
复制
发表时间:
2005-11-01
影响因子:
1.5
通讯作者:
Ullu, E
中科院分区:
文献类型:
--
作者:
Arhin, GK;Shen, SY;Ullu, E
The parasitic protozoa Trypanosoma brucei encodes a full complement of typical eukaryotic small cytoplasmic (sc) and nuclear (sn) RNAs. These include tRNAs, 5S RNA, 7SL RNA and U1, U2, U3, U4, U5 and U6 snRNAs. The latter are involved in different aspects of RNA processing, namely trans-and cis-splicing (U1, U2, U4, U5 and U6), or pre-rRNA maturation (U3). All these RNAs are transcribed by RNA polymerase (pol) III [1], in contrast to most other eukaryotes where U1, U2, U3, U4 and U5 snRNAs are transcribed by RNA pol II. The only known trypanosome snRNA transcribed by pol II is the spliced leader (SL) RNA [2], which donates the SL to all mRNAs via trans-splicing. Newly synthesized pol III transcripts end in a string of uridylates that are subsequently trimmed to generate the mature 3′-end. Soon after synthesis these oligo (U) extensions are bound by the La protein, a nuclear phosphoprotein that has been conserved throughout eukaryotic evolution and protects the 3′-end of nascent pol III RNAs from nuclease degradation [3]. In Saccharomyces cerevisiae, La also forms a complex with RNA polymerase II transcripts such as U1, U2, U3, U4 and U5 snRNAs that end in a polyuridine tract as a result of partial processing of the primary transcripts [4, 5]. For pretRNAs, La is required for the endonucleolytic removal of the 3′ trailer [6], for modulation of 5′-end processing [7] and, as an RNA chaperone, for assisting the correct folding of certain pre-tRNAs [8]. In the case of the U snRNAs, the S. cerevisiae