Relationship between the function and the location of G1 cyclins inS. cerevisiae

2001 ◽  
Vol 114 (24) ◽  
pp. 4599-4611 ◽  
Author(s):  
Nicholas P. Edgington ◽  
Bruce Futcher
Keyword(s):  
Nuclear Localization ◽  
Cellular Localization ◽  
Subcellular Location ◽  
Nuclear Localization Sequence ◽  
Cyclin Dependent Kinase ◽  
Cyclin Dependent Kinases ◽  
G1 Cyclins ◽  
C Terminus ◽  
Localization Sequence ◽  
Nuclear Location

The Saccharomyces cerevisiae cyclin-dependent kinase Cdc28 forms complexes with nine different cyclins to promote cell division. These nine cyclin-Cdc28 complexes have different roles, but share the same catalytic subunit; thus, it is not clear how substrate specificity is achieved. One possible mechanism is specific sub-cellular localization of specific complexes. We investigated the location of two G1 cyclins using fractionation and microscopy. In addition, we developed ‘forced localization’ cassettes, which direct proteins to particular locations, to test the importance of localization. Cln2 was found in both nucleus and cytoplasm. A substrate of Cln2, Sic1, was also in both compartments. Cytoplasmic Cln2 was concentrated at sites of polarized growth. Forced localization showed that some functions of Cln2 required a cytoplasmic location, while other functions required a nuclear location. In addition, one function apparently required shuttling between the two compartments. The G1 cyclin Cln3 required nuclear localization. An autonomous, nuclear localization sequence was found near the C-terminus of Cln3. Our data supports the hypothesis that Cln2 and Cln3 have distinct functions and locations, and the specificity of cyclin-dependent kinases is mediated in part by subcellular location.

scholarly journals The midregion, nuclear localization sequence, and C terminus of PTHrP regulate skeletal development, hematopoiesis, and survival in mice

2010 ◽  
Vol 24 (6) ◽  
pp. 1947-1957 ◽  
Author(s):  
Ramiro E. Toribio ◽  
Holly A. Brown ◽  
Chad M. Novince ◽  
Brandlyn Marlow ◽  
Krista Hernon ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Skeletal Development ◽  
Nuclear Localization Sequence ◽  
C Terminus ◽  
Localization Sequence

scholarly journals Role of Nuclear Pools of Aminoacyl-tRNA Synthetases in tRNA Nuclear Export

2001 ◽  
Vol 12 (5) ◽  
pp. 1381-1392 ◽  
Author(s):  
Abul K. Azad ◽  
David R. Stanford ◽  
Srimonti Sarkar ◽  
Anita K. Hopper
Keyword(s):  
Nuclear Localization ◽  
Nuclear Export ◽  
Trna Synthetase ◽  
Nuclear Localization Sequence ◽  
Sequence Alignments ◽  
Trna Aminoacylation ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Localization Sequence ◽  
Nuclear Location

Reports of nuclear tRNA aminoacylation and its role in tRNA nuclear export ( Lund and Dahlberg, 1998 ; Sarkar et al., 1999 ; Grosshans et al., 2000a ) have led to the prediction that there should be nuclear pools of aminoacyl-tRNA synthetases. We report that in budding yeast there are nuclear pools of tyrosyl-tRNA synthetase, Tys1p. By sequence alignments we predicted a Tys1p nuclear localization sequence and showed it to be sufficient for nuclear location of a passenger protein. Mutations of this nuclear localization sequence in endogenous Tys1p reduce nuclear Tys1p pools, indicating that the motif is also important for nucleus location. The mutations do not significantly affect catalytic activity, but they do cause defects in export of tRNAs to the cytosol. Despite export defects, the cells are viable, indicating that nuclear tRNA aminoacylation is not required for all tRNA nuclear export paths. Because the tRNA nuclear exportin, Los1p, is also unessential, we tested whether tRNA aminoacylation and Los1p operate in alternative tRNA nuclear export paths. No genetic interactions between aminoacyl-tRNA synthetases and Los1p were detected, indicating that tRNA nuclear aminoacylation and Los1p operate in the same export pathway or there are more than two pathways for tRNA nuclear export.

scholarly journals PTHrP Nuclear Localization and Carboxyl Terminus Sequences Modulate Dental and Mandibular Development in Part via the Action of p27

Endocrinology ◽  
2016 ◽  
Vol 2016 (1) ◽  
pp. 72-84 ◽  
Author(s):  
Wen Sun ◽  
Jun Wu ◽  
Linying Huang ◽  
Hong Liu ◽  
Rong Wang ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Alveolar Bone ◽  
Bone Volume ◽  
Carboxyl Terminus ◽  
Nuclear Localization Sequence ◽  
Wild Type ◽  
Mineral Density ◽  
C Terminus ◽  
Localization Sequence ◽  
Dentin Sialoprotein

Abstract To determine whether the action of the PTHrP nuclear localization sequence and C terminus is mediated through p27 in modulating dental and mandibular development, compound mutant mice, which are homozygous for both p27 deletion and the PTHrP1–84 knock-in mutation (p27−/−PthrpKI/KI), were generated. Their teeth and mandibular phenotypes were compared with those of p27−/−, PthrpKUK\ and wild-type mice. At 2 weeks of age, the mandibular mineral density, alveolar bone volume, osteoblast numbers, and dental volume, dentin sialoprotein-immunopo-sitive areas in the first molar were increased significantly in p27−/− mice and decreased dramatically in both PthrpKI/KI and p27−/− PthrpKI/KI mice compared with wild-type mice; however, these parameters were partly rescued in p27−/− PthrpKI/KI mice compared with PthrpKI/KI mice. These data demonstrate that the deletion of p27 in PthrpKI/KI mice can partially rescue defects in dental and mandibular development. Furthermore, we found that deletion of p27 in PthrpKI/KI mice partially corrected the dental and mandibular phenotype by modulating cell cyclin-regulating molecules and antioxidant enzymes. This study therefore indicates that the p27 pathway may function downstream in the action of PTHrP nuclear localization sequence to regulate dental and mandibular development. (Endocrinology 157: 1372–1384, 2016)

scholarly journals Determination of the functional domains involved in nucleolar targeting of nucleolin.

1993 ◽  
Vol 4 (12) ◽  
pp. 1239-1250 ◽  
Author(s):  
L Créancier ◽  
H Prats ◽  
C Zanibellato ◽  
F Amalric ◽  
B Bugler
Keyword(s):  
Rna Binding ◽  
Chimeric Protein ◽  
Nuclear Localization Sequence ◽  
Binding Domains ◽  
Rich Domain ◽  
C Terminus ◽  
N Terminus ◽  
Localization Sequence ◽  
Nuclear Location

Nucleolin (713 aa), a major nucleolar protein, presents two structural domains: a N-terminus implicated in interaction with chromatin and a C-terminus containing four RNA-binding domains (RRMs) and a glycine/arginine-rich domain mainly involved in pre-rRNA packaging. Furthermore, nucleolin was shown to shuttle between cytoplasm and nucleolus. To get an insight on the nature of nuclear and nucleolar localization signals, a set of nucleolin deletion mutants in fusion with the prokaryotic chloramphenicol acetyltransferase (CAT) were constructed, and the resulting chimeric proteins were recognized by anti-CAT antibodies. First, a nuclear location signal bipartite and composed of two short basic stretches separated by eleven residues was characterized. Deletion of either motifs renders the protein cytoplasmic. Second, by deleting one or more domains implicated in nucleolin association either with DNA, RNA, or proteins, we demonstrated that nucleolar accumulation requires, in addition to the nuclear localization sequence, at least two of the five RRMs in presence or absence of N-terminus. However, in presence of only one RRM the N-terminus allowed a partial targeting of the chimeric protein to the nucleolus.

scholarly journals Identification of a nuclear localization sequence within the structure of the human interleukin-1 alpha precursor.

1993 ◽  
Vol 268 (29) ◽  
pp. 22100-22104
Author(s):  
J.H. Wessendorf ◽  
S Garfinkel ◽  
X Zhan ◽  
S Brown ◽  
T Maciag
Keyword(s):  
Nuclear Localization ◽  
Interleukin 1 ◽  
Nuclear Localization Sequence ◽  
Localization Sequence
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