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
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.