Transcription Modulation by a Rat Nuclear Scaffold Protein, P130, and a Rat Highly Repetitive DNA Component or Various Types of Animal and Plant Matrix or Scaffold Attachment Regions

2000 ◽  
Vol 279 (1) ◽  
pp. 282-287 ◽  
Author(s):  
Yasuhide Hibino ◽  
Hiromitsu Ohzeki ◽  
Nobuhiko Sugano ◽  
Koichi Hiraga
Keyword(s):  
Repetitive Dna ◽  
Scaffold Protein ◽  
Nuclear Scaffold ◽  
Transcription Modulation ◽  
Highly Repetitive Dna

Involvement of DNA Methylation in Binding of a Highly Repetitive DNA Component to Nuclear Scaffold Proteins from Rat Liver

1998 ◽  
Vol 252 (2) ◽  
pp. 296-301 ◽  
Author(s):  
Yasuhide Hibino ◽  
Hiromitsu Ohzeki ◽  
Noriko Hirose ◽  
Yasuhiro Morita ◽  
Nobuhiko Sugano
Keyword(s):  
Dna Methylation ◽  
Rat Liver ◽  
Repetitive Dna ◽  
Scaffold Proteins ◽  
Nuclear Scaffold ◽  
Highly Repetitive Dna

A highly repetitive DNA family is dispersed in small clusters throughout the genome

1986 ◽  
Vol 10 (6) ◽  
pp. 486 ◽  
Author(s):  
R BATISTONI ◽  
R VIGNALI ◽  
A NEGRONI ◽  
F CREMISI ◽  
G BARSACCHIPILONE
Keyword(s):  
Repetitive Dna ◽  
Highly Repetitive Dna ◽  
Small Clusters

Sequence Organization of Simple, Highly Repetitive DNA Elements inBrassicaspecies

1991 ◽  
Vol 42 (2) ◽  
pp. 243-249 ◽  
Author(s):  
D. R SIBSON ◽  
S. G. HUGHES ◽  
J. A. BRYANT ◽  
P. N. FITCHETT
Keyword(s):  
Repetitive Dna ◽  
Sequence Organization ◽  
Dna Elements ◽  
Highly Repetitive Dna ◽  
Repetitive Dna Elements

Restriction Endonuclease Analysis of Highly Repetitive DNA as a Phylogenetic Tool

1997 ◽  
Vol 45 (3) ◽  
pp. 332-336 ◽  
Author(s):  
V.V. Grechko ◽  
L.V. Fedorova ◽  
A.N. Fedorov ◽  
S.Ya. Slobodyanyuk ◽  
D.M. Ryabinin ◽  
...  
Keyword(s):  
Restriction Endonuclease ◽  
Repetitive Dna ◽  
Restriction Endonuclease Analysis ◽  
Highly Repetitive Dna ◽  
Endonuclease Analysis

ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders

2009 ◽  
Vol 390 (8) ◽  
Author(s):  
Jemima Barrowman ◽  
Susan Michaelis
Keyword(s):  
Human Health ◽  
Scaffold Protein ◽  
Premature Aging ◽  
Mating Pheromone ◽  
Nuclear Scaffold ◽  
Prelamin A ◽  
Zinc Metalloprotease ◽  
Endoproteolytic Cleavage ◽  
Cleavage Step ◽  
Do So

Abstract ZMPSTE24 is an integral membrane zinc metalloprotease originally discovered in yeast as an enzyme (called Ste24p) required for maturation of the mating pheromone a-factor. Surprisingly, ZMPSTE24 has recently emerged as a key protease involved in human progeroid disorders. ZMPSTE24 has only one identified mammalian substrate, the precursor of the nuclear scaffold protein lamin A. ZMPSTE24 performs a critical endoproteolytic cleavage step that removes the hydrophobic farnesyl-modified tail of prelamin A. Failure to do so has drastic consequences for human health and longevity. Here, we discuss the discovery of the yeast and mammalian ZMPSTE24 orthologs and review the unexpected connection between ZMPSTE24 and premature aging.

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