His-Asp phosphotransfer possibly involved in the nitrogen signal transduction mediated by cytokinin in maize: molecular cloning of cDNAs for two-component regulatory factors and demonstration of phosphotransfer activity in vitro

His-Asp phosphotransfer possibly involved in the nitrogen signal transduction mediated by... Implication of His-to-Asp and/or Asp-to-His (His-Asp) phosphorelay has been recently reported in signal transduction pathways initiated by ethylene and cytokinin. These signaling systems are generally composed of sensor His-protein kinases, His-containing phosphotransfer (HPt) domains, and response regulator domains. In this study, we isolated maize cDNAs, designated as ZmRR2 and ZmHP2, which encode a response regulator domain and HPt domain, respectively, and we identified their His-to-Asp phosphotransfer activity in vitro. The putative translated product of ZmRR2 was highly similar to that of ZmRR1 (78% identity), a maize response regulator homologue. The putative translated product of ZmHP2 showed similarity to that of HPt domains from Arabidopsis thaliana (AHP1–AHP3: 44 to 47% identity) and Saccharomyces cerevisiae (Ypd1p: 24% identity). In vitro experiments demonstrated that the putative signaling factors can transfer the phosphoryl group from His-80 of ZmHP2 to Asp-90 of ZmRRs. Treating detached leaves with t-zeatin or supplying inorganic nitrogen to the whole plant induced the accumulation of ZmRR1 and ZmRR2 transcripts. On the other hand, the steady-state transcript level of ZmHP2 was not affected by cytokinin or inorganic nitrogen sources. These results indicate that His-Asp phosphotransfer may be involved in the transduction of nitrogen signals mediated by cytokinin, and that multiple response regulators participate in the signaling pathways. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

His-Asp phosphotransfer possibly involved in the nitrogen signal transduction mediated by cytokinin in maize: molecular cloning of cDNAs for two-component regulatory factors and demonstration of phosphotransfer activity in vitro

Loading next page...
 
/lp/springer_journal/his-asp-phosphotransfer-possibly-involved-in-the-nitrogen-signal-4ZKCI85uV0
Publisher
Springer Journals
Copyright
Copyright © 1999 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1006391304881
Publisher site
See Article on Publisher Site

Abstract

Implication of His-to-Asp and/or Asp-to-His (His-Asp) phosphorelay has been recently reported in signal transduction pathways initiated by ethylene and cytokinin. These signaling systems are generally composed of sensor His-protein kinases, His-containing phosphotransfer (HPt) domains, and response regulator domains. In this study, we isolated maize cDNAs, designated as ZmRR2 and ZmHP2, which encode a response regulator domain and HPt domain, respectively, and we identified their His-to-Asp phosphotransfer activity in vitro. The putative translated product of ZmRR2 was highly similar to that of ZmRR1 (78% identity), a maize response regulator homologue. The putative translated product of ZmHP2 showed similarity to that of HPt domains from Arabidopsis thaliana (AHP1–AHP3: 44 to 47% identity) and Saccharomyces cerevisiae (Ypd1p: 24% identity). In vitro experiments demonstrated that the putative signaling factors can transfer the phosphoryl group from His-80 of ZmHP2 to Asp-90 of ZmRRs. Treating detached leaves with t-zeatin or supplying inorganic nitrogen to the whole plant induced the accumulation of ZmRR1 and ZmRR2 transcripts. On the other hand, the steady-state transcript level of ZmHP2 was not affected by cytokinin or inorganic nitrogen sources. These results indicate that His-Asp phosphotransfer may be involved in the transduction of nitrogen signals mediated by cytokinin, and that multiple response regulators participate in the signaling pathways.

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 16, 2004

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off