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'''Dehydrin''' (DHN) is a multi-family of [[protein]]s present in [[plants]] that is produced in response to cold and drought stress.<ref>{{cite journal |author=Puhakainen T, Hess MW, Mäkelä P, Svensson J, Heino P, Palva ET |title=Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis |journal=Plant Molecular Biology |volume=54 |issue=5 |pages=743–53 |year=2004 |month=March |pmid=15356392 |doi=10.1023/B:PLAN.0000040903.66496.a4}}</ref> DHNs are [[hydrophilic]] and reliably thermostable. They are stress proteins with a high number of charged [[amino acids]] that belong to the Group II Late Embryogenesis Abundant ([[LEA]]) family”.<ref>{{cite journal |author= Yang Y, He M, Zhu Z, Li S. Xu Y, Zhang C, Singer S, Wang Y |title= Identification of the dehydrin gene family from grapevine species and analysis of their responsiveness of various forms of abiotic and biotic stress |journal= BMC Plant Biology |volume=54 |issue=5 |pages=743–53 |year=2012 |doi=10.1186/1471-2229-12-140 }}</ref> DHNs are primarily found in the [[cytoplasm]] and [[nucleus]] but more recently, they have been found in other [[organelle]]s, like mitochondria and chloroplasts.<ref>{{cite journal |author=Rorat T|title=Plant dehydrins—tissue location, structure and function |journal=Cell and Molecular Biology Letters |volume=11 |issue=4 |pages=536–56 |year=2006 |month=January |pmid=16983453}}</ref> <ref>{{cite journal |author=Saavedra L, Svensson J, Carballo V, Izmendi D, Welin B, Vidal S |title=A dehydrin gene in Physcomitrella patens is required for salt and osmotic stress tolerance |journal=The Plant Journal |volume=45 |issue=2 |pages=237–49 |year=2006 |month=January |pmid=16367967 |doi=10.1111/j.1365-313X.2005.02603.x}}</ref> DHNs are characterized by the presence of [[Glycine]] and other polar [[amino acid]]s. [5] “All DHNs contain at least one copy of a consensus 15-amino acid sequence. The “K segment, The K segment is a Lysine-rich 15-amino acid [[consensus sequence]] (EKKGIMDKIKEKPLG) that is highly conserved in all plants” [6].
'''Dehydrin''' (DHN) is a multi-family of [[protein]]s present in [[plants]] that is produced in response to cold and drought stress.<ref>{{cite journal |author=Puhakainen T, Hess MW, Mäkelä P, Svensson J, Heino P, Palva ET |title=Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis |journal=Plant Molecular Biology |volume=54 |issue=5 |pages=743–53 |year=2004 |month=March |pmid=15356392 |doi=10.1023/B:PLAN.0000040903.66496.a4}}</ref> DHNs are [[hydrophilic]] and reliably thermostable. They are stress proteins with a high number of charged [[amino acids]] that belong to the Group II Late Embryogenesis Abundant ([[LEA]]) family”.<ref>{{cite journal |author= Yang Y, He M, Zhu Z, Li S. Xu Y, Zhang C, Singer S, Wang Y |title= Identification of the dehydrin gene family from grapevine species and analysis of their responsiveness of various forms of abiotic and biotic stress |journal= BMC Plant Biology |volume=54 |issue=5 |pages=743–53 |year=2012 |doi=10.1186/1471-2229-12-140 }}</ref> DHNs are primarily found in the [[cytoplasm]] and [[nucleus]] but more recently, they have been found in other [[organelle]]s, like mitochondria and chloroplasts.<ref>{{cite journal |author=Rorat T|title=Plant dehydrins—tissue location, structure and function |journal=Cell and Molecular Biology Letters |volume=11 |issue=4 |pages=536–56 |year=2006 |month=January |pmid=16983453}}</ref> <ref>{{cite journal |author=Saavedra L, Svensson J, Carballo V, Izmendi D, Welin B, Vidal S |title=A dehydrin gene in Physcomitrella patens is required for salt and osmotic stress tolerance |journal=The Plant Journal |volume=45 |issue=2 |pages=237–49 |year=2006 |month=January |pmid=16367967 |doi=10.1111/j.1365-313X.2005.02603.x}}</ref> DHNs are characterized by the presence of [[Glycine]] and other polar [[amino acid]]s.<ref>{{cite journal |author= Chang-Cai Liu |title= Genome-wide Identification and Charactereization of a Dehydrin Gene Family in Poplar (Populis trichocarpa). |journal= Plant Molecular Biology Reporter |volume=30 |issue=4 |pages=536–56 |year=2012 |doi=10.1007/s11105-011-0395-1}}</ref> All DHNs contain at least one copy of a consensus 15-amino acid sequence. The “K segment, The K segment is a Lysine-rich 15-amino acid [[consensus sequence]] (EKKGIMDKIKEKPLG) that is highly conserved in all plants” [6].


Dehydration-induced [[protein]]s in plants were first observed in 1989, in a comparison of barley and corn [[cDNA]] from plants under [[drought]] conditions.<ref>{{cite journal |author=Close TJ, Kortt AA, Chandler PM |title=A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn |journal=Plant Molecular Biology |volume=13 |issue=1 |pages=95–108 |year=1989 |month=July |pmid=2562763}}</ref> The protein has since been referred to as dehydrin and has been the identified as the genetic basis of [[drought tolerance]] in plants. However, the first direct genetic evidence of dehydrin playing a role in cellular protection during [[osmotic shock]] was not observed until 2005, in the moss, [[Physcomitrella patens]]. In order to show a direct correlation between DHN and stress recovery, a knockout gene was created, which interfered with DHNA’s functionality. After being placed in an environment with salt and osmotic stress and then later being returned to a standard growth medium, the P. patens wildtype was able to recover to 94% of its fresh weight while the P. patens mutant only reached 39% of its fresh weight. This study also concludes that DHN production allows plants to function in high salt concentrations. [4] Another study found evidence of DHN’s impact in drought-stress recovery by showing that [[transcription]] levels of a DHN increased in a drought-tolerant pine, Pinus pisaster, when placed in a drought treatment. However, transcription levels of a DHN decreased in the same drought treatment in a drought-sensitive P. pisaster. Drought-tolerance is a complex trait, thus that it cannot be genetically analyzed as a single gene trait. [8] The exact mechanism of drought tolerance is yet to be determined and is still being researched. One chemical mechanism related to DHN production is the presence of the phytohormone ABA. “A common element in response to many environmental stresses is cellular dehydration. It, in turn, induces biosynthesis of abscisic acid ([[ABA]]), which is well known as a stress hormone because of its rapid and massive accumulation under water stress conditions and participating in stress signal transduction pathways” [9] ABA has been shown to increase the production of DHN, which provides more evidence of a link between DHN and drought tolerance. [9]
Dehydration-induced [[protein]]s in plants were first observed in 1989, in a comparison of barley and corn [[cDNA]] from plants under [[drought]] conditions.<ref>{{cite journal |author=Close TJ, Kortt AA, Chandler PM |title=A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn |journal=Plant Molecular Biology |volume=13 |issue=1 |pages=95–108 |year=1989 |month=July |pmid=2562763}}</ref> The protein has since been referred to as dehydrin and has been the identified as the genetic basis of [[drought tolerance]] in plants. However, the first direct genetic evidence of dehydrin playing a role in cellular protection during [[osmotic shock]] was not observed until 2005, in the moss, [[Physcomitrella patens]]. In order to show a direct correlation between DHN and stress recovery, a knockout gene was created, which interfered with DHNA’s functionality. After being placed in an environment with salt and osmotic stress and then later being returned to a standard growth medium, the P. patens wildtype was able to recover to 94% of its fresh weight while the P. patens mutant only reached 39% of its fresh weight. This study also concludes that DHN production allows plants to function in high salt concentrations. [4] Another study found evidence of DHN’s impact in drought-stress recovery by showing that [[transcription]] levels of a DHN increased in a drought-tolerant pine, Pinus pisaster, when placed in a drought treatment. However, transcription levels of a DHN decreased in the same drought treatment in a drought-sensitive P. pisaster. Drought-tolerance is a complex trait, thus that it cannot be genetically analyzed as a single gene trait. [8] The exact mechanism of drought tolerance is yet to be determined and is still being researched. One chemical mechanism related to DHN production is the presence of the phytohormone ABA. “A common element in response to many environmental stresses is cellular dehydration. It, in turn, induces biosynthesis of abscisic acid ([[ABA]]), which is well known as a stress hormone because of its rapid and massive accumulation under water stress conditions and participating in stress signal transduction pathways” [9] ABA has been shown to increase the production of DHN, which provides more evidence of a link between DHN and drought tolerance. [9]

Revision as of 00:37, 7 December 2012

Dehydrin
Identifiers
SymbolDehydrin
PfamPF00257
InterProIPR000167
PROSITEPS00315
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Dehydrin (DHN) is a multi-family of proteins present in plants that is produced in response to cold and drought stress.[1] DHNs are hydrophilic and reliably thermostable. They are stress proteins with a high number of charged amino acids that belong to the Group II Late Embryogenesis Abundant (LEA) family”.[2] DHNs are primarily found in the cytoplasm and nucleus but more recently, they have been found in other organelles, like mitochondria and chloroplasts.[3] [4] DHNs are characterized by the presence of Glycine and other polar amino acids.[5] All DHNs contain at least one copy of a consensus 15-amino acid sequence. The “K segment, The K segment is a Lysine-rich 15-amino acid consensus sequence (EKKGIMDKIKEKPLG) that is highly conserved in all plants” [6].

Dehydration-induced proteins in plants were first observed in 1989, in a comparison of barley and corn cDNA from plants under drought conditions.[6] The protein has since been referred to as dehydrin and has been the identified as the genetic basis of drought tolerance in plants. However, the first direct genetic evidence of dehydrin playing a role in cellular protection during osmotic shock was not observed until 2005, in the moss, Physcomitrella patens. In order to show a direct correlation between DHN and stress recovery, a knockout gene was created, which interfered with DHNA’s functionality. After being placed in an environment with salt and osmotic stress and then later being returned to a standard growth medium, the P. patens wildtype was able to recover to 94% of its fresh weight while the P. patens mutant only reached 39% of its fresh weight. This study also concludes that DHN production allows plants to function in high salt concentrations. [4] Another study found evidence of DHN’s impact in drought-stress recovery by showing that transcription levels of a DHN increased in a drought-tolerant pine, Pinus pisaster, when placed in a drought treatment. However, transcription levels of a DHN decreased in the same drought treatment in a drought-sensitive P. pisaster. Drought-tolerance is a complex trait, thus that it cannot be genetically analyzed as a single gene trait. [8] The exact mechanism of drought tolerance is yet to be determined and is still being researched. One chemical mechanism related to DHN production is the presence of the phytohormone ABA. “A common element in response to many environmental stresses is cellular dehydration. It, in turn, induces biosynthesis of abscisic acid (ABA), which is well known as a stress hormone because of its rapid and massive accumulation under water stress conditions and participating in stress signal transduction pathways” [9] ABA has been shown to increase the production of DHN, which provides more evidence of a link between DHN and drought tolerance. [9]

There are other proteins in the cell that play a similar role in the recovery of drought treated plants. These proteins are considered dehydrin-like or dehydrin-related. They are poorly defined, in that these dehydrin-like proteins are similar to DHNs, but are unfit to be classified as DHNs for varying reasons. [10] They are found to be similar in that they respond to some or all of the same environmental stresses that induce DHN production. In a particular study dehydrin-like proteins found in the mitochondria were upregulated in drought and cold treatments of cereals.[9]


See also

Antifreeze protein

References

  1. ^ Puhakainen T, Hess MW, Mäkelä P, Svensson J, Heino P, Palva ET (2004). "Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis". Plant Molecular Biology. 54 (5): 743–53. doi:10.1023/B:PLAN.0000040903.66496.a4. PMID 15356392. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ Yang Y, He M, Zhu Z, Li S. Xu Y, Zhang C, Singer S, Wang Y (2012). "Identification of the dehydrin gene family from grapevine species and analysis of their responsiveness of various forms of abiotic and biotic stress". BMC Plant Biology. 54 (5): 743–53. doi:10.1186/1471-2229-12-140.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  3. ^ Rorat T (2006). "Plant dehydrins—tissue location, structure and function". Cell and Molecular Biology Letters. 11 (4): 536–56. PMID 16983453. {{cite journal}}: Unknown parameter |month= ignored (help)
  4. ^ Saavedra L, Svensson J, Carballo V, Izmendi D, Welin B, Vidal S (2006). "A dehydrin gene in Physcomitrella patens is required for salt and osmotic stress tolerance". The Plant Journal. 45 (2): 237–49. doi:10.1111/j.1365-313X.2005.02603.x. PMID 16367967. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  5. ^ Chang-Cai Liu (2012). "Genome-wide Identification and Charactereization of a Dehydrin Gene Family in Poplar (Populis trichocarpa)". Plant Molecular Biology Reporter. 30 (4): 536–56. doi:10.1007/s11105-011-0395-1.
  6. ^ Close TJ, Kortt AA, Chandler PM (1989). "A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn". Plant Molecular Biology. 13 (1): 95–108. PMID 2562763. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

External links