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Cho, Moo Je
Ulsan National Institute of Science and Technology
Research Interests
  • Calcium Signaling
  • Calmodulin
  • Plant Defense Mechanism

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Molecular cloning and functional characterization of a cDNA encoding nucleosome assembly protein 1 (NAP-1) from soybean

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Title
Molecular cloning and functional characterization of a cDNA encoding nucleosome assembly protein 1 (NAP-1) from soybean
Author
Yoon, HWKim, MCLee, SYHwang, IBahk, JDHong, JCIshimi, YCho, Moo Je
Issue Date
1995-12
Publisher
Springer Verlag
Citation
MOLECULAR AND GENERAL GENETICS, v.249, no.5, pp.465 - 473
Abstract
NAP-1, a protein first isolated from mammalian cells, can introduce supercoils into relaxed circular DNA in the presence of purified core histones. Based on its in vitro activity, it has been suggested that NAP-1 may be involved in nucleosome assembly in vivo. We isolated a cDNA clone encoding a soybean NAP-I homolog, SNAP-1. The SNAP-1 cDNA contains an open reading frame of 358 amino acid residues with a calculated molecular weight of 41kDa. The deduced amino acid sequence of SNAP-1 shares sequence similarity with yeast NAP-1 (38%) and human hNRP (32%). Notable features of the deduced sequence are two extended acidic regions thought to be involved in histone binding. SNAP-1 expressed in Escherichia coli induces supercoiling in relaxed circular DNA, suggesting that SNAP-I may have nucleosome assembly activity. The specific activity of SNAP-1 is comparable to that of HeLa NAP-1 in an in vitro assay. Western analysis reveals that SNAP-I is expressed in the immature and young tissues that were examined, while mature tissues such as old leaves and roots, show very little or no expression. NAP-1 homologs also appear to be present in other plant species.
URI
https://scholarworks.unist.ac.kr/handle/201301/6381
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0029563615
DOI
10.1007/BF00290572
ISSN
0026-8925
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BIO_Journal Papers
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