Difference between revisions of "Os04g0473900"

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===Function===
 
===Function===
 
This gene is regarded as ''DWA1''.Putative ''DWA1'' plays important roles in drought resistance.The ''DWA1'' is composed of seven exons(Fig.1) The open reading fame (7,176 bp) encodes a protein consisting of 2,391 aa in ''japonica'' rice, Nipponbare, which is one of the 30 megaproteins (>2,300 aa) predicted in the rice genome<ref name="ref1"/>.DWA1,likely to a megaenzyme,has five domains at least. The N terminus of DWA1 is an oxidoreductase-like domain,and closely followed by the AMP-binding domain(A domain)Then,two repeats of a phosphopantetheine-binding subdomain follow the A domain and feature a thiolation domain (T domain).An allene oxide synthase (AOS)-like domain is located between the second and third repeats of the left-handed β-helix (LbH) domain at the C-terminal region<ref name="ref1"/>.
 
This gene is regarded as ''DWA1''.Putative ''DWA1'' plays important roles in drought resistance.The ''DWA1'' is composed of seven exons(Fig.1) The open reading fame (7,176 bp) encodes a protein consisting of 2,391 aa in ''japonica'' rice, Nipponbare, which is one of the 30 megaproteins (>2,300 aa) predicted in the rice genome<ref name="ref1"/>.DWA1,likely to a megaenzyme,has five domains at least. The N terminus of DWA1 is an oxidoreductase-like domain,and closely followed by the AMP-binding domain(A domain)Then,two repeats of a phosphopantetheine-binding subdomain follow the A domain and feature a thiolation domain (T domain).An allene oxide synthase (AOS)-like domain is located between the second and third repeats of the left-handed β-helix (LbH) domain at the C-terminal region<ref name="ref1"/>.
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== '''Mutation''' ==
 
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[[File:图片3.png|right|thumb|200px|Identification of the drought-hypersensitive ''dwa1'' mutant in rice, in which functional complementation of ''dwa1'' restore the drought resistance(from reference<ref name="ref1" />)]]
 
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'''(1)'''There is an insertion of T-DNA in the sixth exon of ''DWA1'' (Fig.1A).<br>
 
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'''(2)'''RT-qPCR analysis of ''DWA1'' in WT and mutant tissues(leaf and panicle) indicate that ''dwa1'' is a loss of-function mutant because of no transcript found in the mutant(Fig.1B).<br>
 
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'''(3)'''During the course of drought treatment, the mutant wilted and exhibited leaf rolling earlier than the WT.After severe drought treatment followed by rewatering, more than 90% of the WT plants survive, whereas the ''dwa1'' mutant plants are almost dead(Fig.1C and D).<br>
 
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'''(4)'''Water loss rate of mutant is faster than WT(Fig.1E).<br>
 
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'''(5)'''DWA1-functional complementation(DWA1-FC)lines which is inserted the full-length genomic fragment of ''DWA1'' into the ''dwa1'' mutant restore drought resistance(Fig.1F and G).<br>
 
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'''(6)'''Plant height at the reproductive stage are also restored in the DWA1-FC lines(Fig.1H).
 
  
  

Revision as of 12:56, 23 May 2014

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Annotated Information

Function

This gene is regarded as DWA1.Putative DWA1 plays important roles in drought resistance.The DWA1 is composed of seven exons(Fig.1) The open reading fame (7,176 bp) encodes a protein consisting of 2,391 aa in japonica rice, Nipponbare, which is one of the 30 megaproteins (>2,300 aa) predicted in the rice genome[1].DWA1,likely to a megaenzyme,has five domains at least. The N terminus of DWA1 is an oxidoreductase-like domain,and closely followed by the AMP-binding domain(A domain)Then,two repeats of a phosphopantetheine-binding subdomain follow the A domain and feature a thiolation domain (T domain).An allene oxide synthase (AOS)-like domain is located between the second and third repeats of the left-handed β-helix (LbH) domain at the C-terminal region[1].


Expression

Evolution

Unrooted phylogenetic tree and domain architecture of DWA1 protein orthologs in vascular plants and microbial relatives(from reference[1])

At present,homologous sequences with DWA1are all from microorganisms.Nonribosomal peptide synthetase(NRPS),a megaenzyme needed for nonribosomal peptides synthesis in bacteria and filamentous fungi[2],is a major branch of the AMP-binding enzyme superfamily.More importantly,both these homologous sequences and DWA1have an NRPS module, including adenylation domain, followed by a thiolation domain catalyzing the activation and thiolation reaction of an amino acid instead of a carboxyl substrate for acyl-CoA synthetase.These features suggest that DWA1 and its plant homologs may be derived from a prokaryotic NRPS rather than the acyl-CoA synthetase family, which possesses only the A domain[1].

Labs working on this gene

  • National Key Laboratory of Crop Genetic Improvement, National Center of Plant Gene Research (Wuhan), Huazhong Agricultural University, Wuhan,China

References

<references> [1]

[2]
  1. ↑ 1.0 1.1 1.2 1.3 1.4 Xiaoyi Zhu, Lizhong Xiong.（2013）Putative megaenzyme DWA1 plays essential roles in drought resistance by regulating stress-induced wax deposition in rice.PANS 110(44): 17790-17795.
  2. ↑ 2.0 2.1 Marahiel MA, Stachelhaus T, Mootz HD.(1997) Modular peptide synthetases involved in nonribosomal peptide synthesis.Chem Rev 97(7):2651–2674.
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