Functional modules in ribosomal protein L5 for ribonucleoprotein complex formation and nucleocytoplasmic transport

Citation
M. Claussen et al., Functional modules in ribosomal protein L5 for ribonucleoprotein complex formation and nucleocytoplasmic transport, J BIOL CHEM, 274(48), 1999, pp. 33951-33958
Citations number
89
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
274
Issue
48
Year of publication
1999
Pages
33951 - 33958
Database
ISI
SICI code
0021-9258(19991126)274:48<33951:FMIRPL>2.0.ZU;2-C
Abstract
Ribosomal protein L5 forms a small, extraribosomal complex with 5 S ribosom al RNA, referred to as the 5 S ribonucleoprotein complex, which shuttles be tween nucleus and cytoplasm in Xenopus oocytes, Mapping elements in L5 that mediate nuclear protein import defines three separate such activities (L5- nuclear localization sequence (NLS)-1, -2, and -3), which are functional in both oocytes and somatic cells, RNA binding activity involves N-terminal a s well as C-terminal elements of L5, In contrast to the full length protein , none of the individual NLSs carrying L5 fragments are able to allow for t he predominating accumulation in the nucleoli that is observed with the ful l-length protein. The separate L5-NLSs differ in respect to two activities. Firstly, only L5-NLS-1 and -3, not L5-NLS-2, are capable of promoting the nuclear transfer of a heterologous, covalently attached ribonucleoprotein c omplex. Secondly, only L5-NLS-1 is able to bind strongly to a variety of di fferent import receptors; those that recognize L5-NLS-2 and -3 have yet to be identified.