作者: Peter J. Schaap , Jan van't Riet , Conrad L. Woldringh , Hendrik A. Raué
DOI: 10.1016/0022-2836(91)80216-H
关键词: Ribosomal protein 、 Nuclear cap-binding protein complex 、 Nuclear transport 、 Ribosomal RNA 、 Protein subunit 、 Nuclear localization sequence 、 Nuclear protein 、 Biochemistry 、 Saccharomyces cerevisiae 、 Biology
摘要: Abstract The regions of the large subunit ribosomal protein L25 from SAccharomyces cerevisiae responsible for nuclear localization were identified by constructing fusion genes encoding various segments linked to amino terminus β-galactosidase. Indirect immunofluorescence yeast cells expressing fusions demonstrated that acid residues 1 17 as well 18 41 promote import reporter into nucleus. Both signal (NLS) sequences appear consist two distinct functional parts: one showed relatively weak targeting activity, whereas other considerably enhances this activity but does not itself. Microinjection in vitro prepared intact and N-terminally truncated Xenopus laevis oocytes region containing NLS is indeed required efficient protein. This conclusion was confirmed complementation experiments using a strain conditionally expresses wild-type L25. latter also indicated are full 60 S subunits. Yeast forms lack viable, show impaired growth highly abnormal cell morphology.