Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
0  structures 182  species 0  interactions 1293  sequences 12  architectures

Family: Dehydrin (PF00257)

Summary: Dehydrin

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Dehydrin". More...

Dehydrin Edit Wikipedia article

Dehydrin
Identifiers
Symbol Dehydrin
Pfam PF00257
InterPro IPR000167
PROSITE PS00315

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.[7] 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.[8] 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.[9] 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. One common response to environmental stresses is process known as cellular dehydration. Cellular dehydration induces biosynthesis of abscisic acid (ABA), which is known to react as a stress hormone because of its accumulation in the plant under water stress conditions. ABA also participates in stress signal transduction pathways ABA has been shown to increase the production of DHN, which provides more evidence of a link between DHN and drought tolerance.[10]

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.[11] 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.[12]

See also[edit]

References[edit]

  1. ^ Puhakainen T, Hess MW, Mäkelä P, Svensson J, Heino P, Palva ET (March 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. 
  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. 
  3. ^ Rorat T (January 2006). "Plant dehydrins—tissue location, structure and function". Cell and Molecular Biology Letters 11 (4): 536–56. doi:10.2478/s11658-006-0044-0. PMID 16983453. 
  4. ^ Saavedra L, Svensson J, Carballo V, Izmendi D, Welin B, Vidal S (January 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. 
  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): 848–59. doi:10.1007/s11105-011-0395-1. 
  6. ^ Wilkens S, Close T (2003). "The binding of Maize DHN1 to Lipid Vesicles. Gain of Structure and Specificity". Plant Physiol 131 (1): 309–16. doi:10.1104/pp.011171. 
  7. ^ Close TJ, Kortt AA, Chandler PM (July 1989). "A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn". Plant Molecular Biology 13 (1): 95–108. PMID 2562763. 
  8. ^ Saavedra L, Svensson J, Carballo V, Izmendi D, Welin B, Vidal S (January 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. 
  9. ^ Velasco-Conde T, Yakovlev I, Majada J, Aranda I, Johnsen O (2012). "Dehydrins in maritine pine (Pinus pinaster) and their expression related to drought stress response". Tree Genetics and Genomes 8 (5): 957–73. doi:10.1007/s11295-012-0476-9. 
  10. ^ Borovskii G, Stupnikova I, Antipina A, Vladimirova S, Voinikov V (2002). "Accumulation of dehydrin-like proteins in the mitochondria of cereals in response to cold, freezing, drought and ABA treatment". BMC Plant Biology 2 (5). doi:10.1186/1471-2229-2-5. 
  11. ^ Rurek M. "Diverse accumulation of several dehydrin-like proteins in cauliflower (Brassica oleracea var. botrytis), Arabidopsis thaliana and yellow lupin (Lupinus luteus) mitochondria under cold and heat stress". BMC Plant Biology 10 (181): 309–16. doi:10.1186/1471-2229-10-181. 
  12. ^ Borovskii G, Stupnikova I, Antipina A, Vladimirova S, Voinikov V (2002). "Accumulation of dehydrin-like proteins in the mitochondria of cereals in response to cold, freezing, drought and ABA treatment". BMC Plant Biology 2 (5). doi:10.1186/1471-2229-2-5. 

External links[edit]

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Dehydrin Provide feedback

No Pfam abstract.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000167

A number of proteins are produced by plants that experience water-stress. Water-stress takes place when the water available to a plant falls below a critical level. The plant hormone abscisic acid (ABA) appears to modulate the response of plant to water-stress. Proteins that are expressed during water- stress are called dehydrins [PUBMED:2562763, PUBMED:1387328]. Dehydrins contribute to freezing stress tolerance in plants and it was suggested that this could be partly due to their protective effect on membranes [PUBMED:15356392].

Dehydrins share a number of structural features. One of the most notable features is the presence, in their central region, of a continuous run of five to nine serines followed by a cluster of charged residues. Such a region has been found in all known dehydrins so far with the exception of pea dehydrins. A second conserved feature is the presence of two copies of a lysine-rich octapeptide; the first copy is located just after the cluster of charged residues that follows the poly-serine region and the second copy is found at the C-terminal extremity.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

Loading domain graphics...

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(27)
Full
(1293)
Representative proteomes NCBI
(1285)
Meta
(0)
RP15
(23)
RP35
(58)
RP55
(87)
RP75
(114)
Jalview View  View  View  View  View  View  View   
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(27)
Full
(1293)
Representative proteomes NCBI
(1285)
Meta
(0)
RP15
(23)
RP35
(58)
RP55
(87)
RP75
(114)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(27)
Full
(1293)
Representative proteomes NCBI
(1285)
Meta
(0)
RP15
(23)
RP35
(58)
RP55
(87)
RP75
(114)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite & Pfam-B_3306 (Release 7.5)
Previous IDs: dehydrin;
Type: Family
Author: Finn RD, Bateman A
Number in seed: 27
Number in full: 1293
Average length of the domain: 110.70 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 87.32 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.7 21.7
Trusted cut-off 21.8 21.7
Noise cut-off 21.6 21.6
Model length: 153
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.