Late embryogenesis abundant proteins

Late embryogenesis abundant proteins (LEA proteins) are proteins in plants, some bacteria, and invertebrates that protect against protein aggregation due to desiccation or osmotic stresses associated with low temperature.[1][2][3] LEA proteins were initially discovered accumulating late in embryogenesis of cotton seeds.[4] Originally noticed due to its abundance in seeds and pollens,[2] LEA proteins have been found to protect against desiccation, cold, or high salinity in a variety of organisms, including the bacterium Deinococcus radiodurans, nematode Caenorhabditis elegans, Artemia (brine shrimp), and rotifers.[5][6]

Function

LEA proteins function by mechanisms which are distinct from those displayed by heat shock molecular chaperones.[1] Although the causes of LEA protein induction have not yet been determined, conformational changes in transcription factors or integral membrane proteins due to water loss have been suggested.[7] LEA proteins are particularly protective of mitochondrial membranes against dehydration damage.[8]

Types

LEA proteins are grouped by sequence similarity into 5 or 7 major groups, with 9 to 14 subgroups. There is also a simplistic scheme that groups by origin, i.e. plant, bacterial, and animal.[9] The groups are:[10][11]

Nomenclature of LEA families[10]
Pfam Battaglia Bray Dure Bies-Ethève Names
Dehydrin (PF00257) 2 2 D-11 2 Dehydrin, RAB
SMP (PF04927) 5A 6 D-34 5 PAP140
LEA_1 (PF03760) 4A 4 N/a 4 LE25_LYCES
4B D-113 PAP260, PAP051
LEA_2 (PF03168) 5C N/a D-95 7 LEA14, WHy domain[9]
LEA_3 (PF03242) 5B N/a D-73 6 AtD121, Sag21, lea5
LEA_4 (PF02987) 3A 3 D-7 3 ECP63, PAP240, PM27
3B 5→3 D-29 D-29
LEA_5 (PF00477) 1 1 D-19 1 Em1, Em6
LEA_6 (PF10714) 6 N/a N/a 8 LEA18
AWA_WDS (PF02496) 7 N/a N/a N/a ASR

One reason there are so many different families is that the LEA proteins were originally noticed by their common compositional and biophysical features (hydrophilic, high glycine), not by a united ancestry. There are many additional families that also share these features but they are not as common in plants.[10] According to LEAPdb, the Pfam classification is the most comprehensive.[11]

Applications

A group 3 (LEA_4) small LEA protein can be used to protect Cryo-EM samples from air-water interface damage (preferred orientation, complex dissociation, and protein denaturation) during freezing. They physically keep the sample molecules away from the air-water interface.[12]

See also

References

  1. ^ a b Goyal, K., Walton, L. J., & Tunnacliffe, A. (2005). "LEA proteins prevent protein aggregation due to water stress". Biochemical Journal. 388 (Part 1): 151–157. doi:10.1042/BJ20041931. PMC 1186703. PMID 15631617.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ a b Hundertmark M, Hincha DK (2008). "LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana". BMC Genomics. 9: 118. doi:10.1186/1471-2164-9-118. PMC 2292704. PMID 18318901.
  3. ^ Liu, Y; Chakrabortee, S; Li, R; Zheng, Y; Tunnacliffe, A (18 February 2011). "Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine-dependent protein aggregation". FEBS Letters. 585 (4): 630–4. Bibcode:2011FEBSL.585..630L. doi:10.1016/j.febslet.2011.01.020. PMID 21251910. S2CID 23589368.
  4. ^ Dure L 3rd, Greenway SC, Galau GA (1981). "Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis". Biochemistry. 20 (14): 4162–4168. doi:10.1021/bi00517a033. PMID 7284317.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: numeric names: authors list (link)
  5. ^ Gal TZ, Glazer I, Koltai H (2004). "An LEA group 3 family member is involved in survival of C. elegans during exposure to stress". FEBS Letters. 577 (1–2): 21–26. Bibcode:2004FEBSL.577...21G. doi:10.1016/j.febslet.2004.09.049. PMID 15527756. S2CID 21960486.
  6. ^ Menze MA, Boswell L, Toner M, Hand SC (2009). "Occurrence of mitochondria-targeted Late Embryogenesis Abundant (LEA) gene in animals increases organelle resistance to water stress". Journal of Biological Chemistry. 284 (16): 10714–10719. doi:10.1074/jbc.C900001200. PMC 2667758. PMID 19228698.
  7. ^ Caramelo JJ, Iusem ND (2009). "When cells lose water: Lessons from biophysics and molecular biology". Progress in Biophysics and Molecular Biology. 99 (1): 1–6. doi:10.1016/j.pbiomolbio.2008.10.001. hdl:11336/25755. PMID 18977383.
  8. ^ Tolleter D, Hincha DK, Macherel D (2010). "A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1798 (10): 1926–1933. doi:10.1016/j.bbamem.2010.06.029. PMID 20637181.
  9. ^ a b Mertens, J; Aliyu, H; Cowan, DA (1 August 2018). "LEA Proteins and the Evolution of the WHy Domain". Applied and environmental microbiology. 84 (15). doi:10.1128/AEM.00539-18. PMC 6052280. PMID 29802195.
  10. ^ a b c Battaglia, M; Olvera-Carrillo, Y; Garciarrubio, A; Campos, F; Covarrubias, AA (September 2008). "The enigmatic LEA proteins and other hydrophilins". Plant physiology. 148 (1): 6–24. doi:10.1104/pp.108.120725. PMC 2528095. PMID 18772351.
  11. ^ a b Hunault, G; Jaspard, E (1 April 2010). "LEAPdb: a database for the late embryogenesis abundant proteins". BMC genomics. 11: 221. doi:10.1186/1471-2164-11-221. PMC 2858754. PMID 20359361.
  12. ^ Abe, Kaitlyn M.; Li, Gan; He, Qixiang; Grant, Timothy; Lim, Ci Ji (4 September 2024). "Small LEA proteins mitigate air-water interface damage to fragile cryo-EM samples during plunge freezing". Nature Communications. 15 (1). doi:10.1038/s41467-024-52091-1.


This article is issued from Wikipedia. The text is available under Creative Commons Attribution-Share Alike 4.0 unless otherwise noted. Additional terms may apply for the media files.