Difference between revisions of "Os02g0115900"

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OsBip1,also named BiP3,has functions to assist folding seed storage proteins and has effect on seed phenotype,seed starch and protein accumulation
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The rice '''''Os02g0115900''''' was reported as '''''BiP''''' in 2009 <ref name="ref1" /> by researchers from Japan.
  
 
==Annotated Information==
 
==Annotated Information==
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===Gene Symbol===
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*'''''Os02g0115900''''' '''''<=>''''' '''''OsBiP1, BiP1, BiP, Bip3, OsBiP3, BIP1/OsBIP3, OsMed37_2, Med37_2'''''
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===Function===
 
===Function===
Binding protein (BiP) is enssential in folding of secretory proteins. Bip has a function in folding seed storage proteins in the ER lumen. ''OsBip1'' reported by Park and his colleagues and ''BiP3'' reported by Wakasa,Yasuda,et al are the same gene.
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* Seed storage proteins are specifi cally and highly synthesized during seed maturation and are deposited into protein bodies (PBs) via the endoplasmic reticulum (ER) lumen.
In rice overpressing BiP1 , XA21-mediated immunity is compromised, XA21 stability is significantly decreased, and XA21 proteolytic cleavage is inhibited. Meanwhile,Wakasa,Yasuda, et al believe that severe suppression (BiP1 KD) or significant over-expression (BiP1 OEmax) of BiP1 can alter seed phenotype and the intracellular structure of endosperm cells and reduce seed storage protein content, starch accumulation and grain weight.
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* The accumulation process is mediated by ER chaperones such as luminal binding protein (BiP) and protein disulfi de isomerase (PDI)
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* The PB-like structure ('''''BiP''''') may be formed in the ER lumen, resulting in inhibition of translation, folding and transport of seed proteins.
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* BiP interacts with nascent immature secretory proteins synthesized from membrane-bound polysomes on the ER,and assists in protein folding in concert with other chaperones and folding helpers such as calnexin and protein disulfide isomerase-like proteins in the ER lumen.  
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* BiP not only participates in assistence of protein folding but also take part in the protein degradation process known as ER-associated degradation.
  
===Expression===
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===Phenotypic analysis===
1. Researchers conclude that the peptides from the 140 kDa proteins can match XA21 from the N-terminal LRR region to the C-terminal kinase domain.However,the peptides from the 110 kDa protein match the LRR, but not the kinase domain.
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* The seed phenotype of the PDI-overexpressing transformant was almost identical to that of the wild type, whereas overexpression of '''''BiP''''' resulted in transgenic rice seed that displayed an opaque phenotype with fl oury and shrunken features.  
2.Gene BiP3,predicted to encode a 666 amino acid protein with a molecular mass of 73.4 kDa ,has a 1,998 bp open reading frame which consists of 7 introns and 8 exons.In overall structure,BiP3 is similar to other known HSP70s in plants and animals.It has an approximately 45 kDa domain at the N-terminus that is predicted to have ATPase activity and a domain of approximately 25 kDa at the C-terminus having a predicted substrate-binding domain.  
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* In the BiP-overexpressing line, the levels of accumulation of seed storage proteins and starch contents were signifi cantly lower compared with the wild type.
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* Interestingly, overproduction of '''''BiP''''' in the endosperm of the transformant not only altered the morphological structure of ER-derived PB-I, but also generated unusual new PB-like structures composed of a high electron density matrix containing glutelin and BiP and a low electron density matrix containing prolamins.
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* Notably, polysomes were attached around the aberrant PB-like structures, indicating that this aberrant structure is an ER-derived PB-I derivative.
  
 
===Evolution===
 
===Evolution===
1.BiP is one of the major ER chaperones and belongs to the heat shock protein 70 (HSP70) family.Rice BiP3 (OsBiP3) shows the greatest similarity to ArabidopsisBiP1 and BiP2 with 89.2% and 89.3% identity.
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* BiP is one of the major ER chaperones and belongs to the heat shock protein 70 (HSP70) family.Rice BiP3 (OsBiP3) shows the greatest similarity to ArabidopsisBiP1 and BiP2 with 89.2% and 89.3% identity.
2.BiP with an ATPase domain at its N-terminus and a protein-binding domain at its C-terminus allows BiP to cycle between ATP hydrolysis and ADP exchange, and it is coupled to binding and release of the unfolded protein.
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* BiP with an ATPase domain at its N-terminus and a protein-binding domain at its C-terminus allows BiP to cycle between ATP hydrolysis and ADP exchange, and it is coupled to binding and release of the unfolded protein.
3.BiP protein has a KDEL ER retention signal at the C-terminus and is retained in the ER lumen. BiP interacts with nascent immature secretory proteins synthesized from membrane-bound polysomes on the ER,and assists in protein folding in concert with other chaperones and folding helpers such as calnexin and protein disulfide isomerase-like proteins in the ER lumen. BiP not only participates in assistence of protein folding but also take part in the protein degradation process known as ER-associated degradation.
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* BiP protein has a KDEL ER retention signal at the C-terminus and is retained in the ER lumen.
4.Scientists reported that over-expression of BiP1 (Os02g0115900) in transgenic rice seed resulted in an opaque phenotype and abnormal intracellular structure.
 
  
 
==Labs working on this gene==
 
==Labs working on this gene==
Transgenic Crop Research and Development Center, National Institute of Agrobiological Sciences;
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* Transgenic Crop Research and Development Center, National Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki, 305-8602 Japan
Department of Plant Pathology, University of California Davis
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* Research Team for Crop Cold Tolerance, National Agricultural Research Center for Hokkaido region, Hitsujigaoka 1, Toyohira-ku, Sapporo,Hokkaido, 062-8555 Japan
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* Rice Biotechnology Research Team, National Institute of Crop Sciences, Kannondai 2-1-18, Tsukuba, Ibaraki, 305-8518 Japan
  
 
==References==
 
==References==
1.Chang-Jin Park; Rebecca Bart; Mawsheng Chern; Patrick E. Canlas; Wei Bai; Pamela C. Ronald.Overexpression of the Endoplasmic Reticulum Chaperone BiP3 Regulates XA21-Mediated Innate Immunity in Rice.PLoS ONE, 2010, 5(2): e9262.
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<references>
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* <ref name="ref1">
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Yasuda H, Hirose S, Kawakatsu T, Wakasa Y, Takaiwa F. Overexpression of BiP
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has inhibitory effects on the accumulation of seed storage proteins in endosperm
 +
cells of rice. Plant Cell Physiol. 2009 Aug;50(8):1532-43. doi:
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10.1093/pcp/pcp098. PubMed PMID: 19567376.
  
2.Yuhya Wakasa; Hiroshi Yasuda; Youko Oono; Taiji Kawakatsu; Sakiko Hirose; Hideyuki Takahashi; Shimpei Hayashi; Lijun Yang; Fumio Takaiwa.Expression of ER quality control-related genes in response to changes in BiP1 levels in developing rice endosperm.The Plant Journal, 2011, 65(5): 675-689.
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</ref>
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</references>
  
 
==Structured Information==
 
==Structured Information==
 
     [[Category:Genes]][[Category:Oryza Sativa Japonica Group]][[Category:Japonica Chromosome 2]]
 
     [[Category:Genes]][[Category:Oryza Sativa Japonica Group]][[Category:Japonica Chromosome 2]]

Latest revision as of 02:17, 8 March 2017

The rice Os02g0115900 was reported as BiP in 2009 [1] by researchers from Japan.

Annotated Information

Gene Symbol

  • Os02g0115900 <=> OsBiP1, BiP1, BiP, Bip3, OsBiP3, BIP1/OsBIP3, OsMed37_2, Med37_2

Function

  • Seed storage proteins are specifi cally and highly synthesized during seed maturation and are deposited into protein bodies (PBs) via the endoplasmic reticulum (ER) lumen.
  • The accumulation process is mediated by ER chaperones such as luminal binding protein (BiP) and protein disulfi de isomerase (PDI)
  • The PB-like structure (BiP) may be formed in the ER lumen, resulting in inhibition of translation, folding and transport of seed proteins.
  • BiP interacts with nascent immature secretory proteins synthesized from membrane-bound polysomes on the ER,and assists in protein folding in concert with other chaperones and folding helpers such as calnexin and protein disulfide isomerase-like proteins in the ER lumen.
  • BiP not only participates in assistence of protein folding but also take part in the protein degradation process known as ER-associated degradation.

Phenotypic analysis

  • The seed phenotype of the PDI-overexpressing transformant was almost identical to that of the wild type, whereas overexpression of BiP resulted in transgenic rice seed that displayed an opaque phenotype with fl oury and shrunken features.
  • In the BiP-overexpressing line, the levels of accumulation of seed storage proteins and starch contents were signifi cantly lower compared with the wild type.
  • Interestingly, overproduction of BiP in the endosperm of the transformant not only altered the morphological structure of ER-derived PB-I, but also generated unusual new PB-like structures composed of a high electron density matrix containing glutelin and BiP and a low electron density matrix containing prolamins.
  • Notably, polysomes were attached around the aberrant PB-like structures, indicating that this aberrant structure is an ER-derived PB-I derivative.

Evolution

  • BiP is one of the major ER chaperones and belongs to the heat shock protein 70 (HSP70) family.Rice BiP3 (OsBiP3) shows the greatest similarity to ArabidopsisBiP1 and BiP2 with 89.2% and 89.3% identity.
  • BiP with an ATPase domain at its N-terminus and a protein-binding domain at its C-terminus allows BiP to cycle between ATP hydrolysis and ADP exchange, and it is coupled to binding and release of the unfolded protein.
  • BiP protein has a KDEL ER retention signal at the C-terminus and is retained in the ER lumen.

Labs working on this gene

  • Transgenic Crop Research and Development Center, National Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki, 305-8602 Japan
  • Research Team for Crop Cold Tolerance, National Agricultural Research Center for Hokkaido region, Hitsujigaoka 1, Toyohira-ku, Sapporo,Hokkaido, 062-8555 Japan
  • Rice Biotechnology Research Team, National Institute of Crop Sciences, Kannondai 2-1-18, Tsukuba, Ibaraki, 305-8518 Japan

References

  1. Yasuda H, Hirose S, Kawakatsu T, Wakasa Y, Takaiwa F. Overexpression of BiP has inhibitory effects on the accumulation of seed storage proteins in endosperm cells of rice. Plant Cell Physiol. 2009 Aug;50(8):1532-43. doi: 10.1093/pcp/pcp098. PubMed PMID: 19567376.

Structured Information