Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea.

Abstract:

:A CDNA encoding a 47 kDa nucleoside triphosphatase (NTPase) that is associated with the chromatin of pea nuclei has been cloned and sequenced. The translated sequence of the cDNA includes several domains predicted by known biochemical properties of the enzyme, including five motifs characteristic of the ATP-binding domain of many proteins, several potential casein kinase II phosphorylation sites, a helix-turn-helix region characteristic of DNA-binding proteins, and a potential calmodulin-binding domain. The deduced primary structure also includes an N-terminal sequence that is a predicted signal peptide and an internal sequence that could serve as a bipartite-type nuclear localization signal. Both in situ immunocytochemistry of pea plumules and immunoblots of purified cell fractions indicate that most of the immunodetectable NTPase is within the nucleus, a compartment proteins typically reach through nuclear pores rather than through the endoplasmic reticulum pathway. The translated sequence has some similarity to that of human lamin C, but not high enough to account for the earlier observation that IgG against human lamin C binds to the NTPase in immunoblots. Northern blot analysis shows that the NTPase MRNA is strongly expressed in etiolated plumules, but only poorly or not at all in the leaf and stem tissues of light-grown plants. Accumulation of NTPase mRNA in etiolated seedlings is stimulated by brief treatments with both red and far-red light, as is characteristic of very low-fluence phytochrome responses. Southern blotting with pea genomic DNA indicates the NTPase is likely to be encoded by a single gene.

journal_name

Plant Mol Biol

journal_title

Plant molecular biology

authors

Hsieh HL,Tong CG,Thomas C,Roux SJ

doi

10.1007/BF00017808

keywords:

["NASA Discipline Number 40-50","NASA Discipline Plant Biology","NASA Program Space Biology","Non-NASA Center"]

subject

Has Abstract

pub_date

1996-01-01 00:00:00

pages

135-47

issue

1

eissn

0167-4412

issn

1573-5028

journal_volume

30

pub_type

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