TY - JOUR
T1 - NSP1
T2 - A yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain
AU - Nehrbass, Ulf
AU - Kern, Hildegard
AU - Mutvei, Ann
AU - Horstmann, Heinz
AU - Marshallsay, Brigitte
AU - Hurt, Eduard C.
N1 - Funding Information:
We are grateful to Dr. J. Kilmartin (Cambridge) for anti-tubulin antibody, Dr. G. Schatz (Basel) for anti-hexokinase antibody and help in electron microscopy, Dr. H. Gausepohl and Dr. R. Frank for peptide synthesis, Dr. G. Griffiths for help in immunoelectron microscopy, and Niamh Hiney for typing the manuscript. E. C. H. was the recipient of a grant from the Deutsche Forschungsgemeinschaft.
PY - 1990/6/15
Y1 - 1990/6/15
N2 - NSP1 is located at the nuclear periphery in yeast and is essential for cell growth. Employing immunoelectron microscopy on yeast cells, we show that NSP1 is located at the nuclear pores. The molecular analysis of the NSP1 protein points to a two domain model: a nonessential domain (the first 603 amino acids) composed of repetitive sequences common to other nuclear proteins and an essential, carboxy-terminal domain (residues 604-823) mediating the vital function of NSP1. The NSP1 carboxy-terminal domain, which shows a heptad repeat organization, affected the correct location of two nuclear proteins: site-specific amino acid substitutions within a predicted α-helical structure of this domain caused a temperature-sensitive growth arrest at 37°C and the appearance of NSP1 and NOP1, a nucleolar protein, in the cytosol.
AB - NSP1 is located at the nuclear periphery in yeast and is essential for cell growth. Employing immunoelectron microscopy on yeast cells, we show that NSP1 is located at the nuclear pores. The molecular analysis of the NSP1 protein points to a two domain model: a nonessential domain (the first 603 amino acids) composed of repetitive sequences common to other nuclear proteins and an essential, carboxy-terminal domain (residues 604-823) mediating the vital function of NSP1. The NSP1 carboxy-terminal domain, which shows a heptad repeat organization, affected the correct location of two nuclear proteins: site-specific amino acid substitutions within a predicted α-helical structure of this domain caused a temperature-sensitive growth arrest at 37°C and the appearance of NSP1 and NOP1, a nucleolar protein, in the cytosol.
UR - http://www.scopus.com/inward/record.url?scp=0025302451&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(90)90063-K
DO - 10.1016/0092-8674(90)90063-K
M3 - Article
C2 - 2112428
AN - SCOPUS:0025302451
SN - 0092-8674
VL - 61
SP - 979
EP - 989
JO - Cell
JF - Cell
IS - 6
ER -