Document Detail


Unique amino acid signatures that are evolutionarily conserved distinguish simple-type, epidermal and hair keratins.
MedLine Citation:
PMID:  22215855     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Keratins (Ks) consist of central α-helical rod domains that are flanked by non-α-helical head and tail domains. The cellular abundance of keratins, coupled with their selective cell expression patterns, suggests that they diversified to fulfill tissue-specific functions although the primary structure differences between them have not been comprehensively compared. We analyzed keratin sequences from many species: K1, K2, K5, K9, K10, K14 were studied as representatives of epidermal keratins, and compared with K7, K8, K18, K19, K20 and K31, K35, K81, K85, K86, which represent simple-type (single-layered or glandular) epithelial and hair keratins, respectively. We show that keratin domains have striking differences in their amino acids. There are many cysteines in hair keratins but only a small number in epidermal keratins and rare or none in simple-type keratins. The heads and/or tails of epidermal keratins are glycine and phenylalanine rich but alanine poor, whereas parallel domains of hair keratins are abundant in prolines, and those of simple-type epithelial keratins are enriched in acidic and/or basic residues. The observed differences between simple-type, epidermal and hair keratins are highly conserved throughout evolution. Cysteines and histidines, which are infrequent keratin amino acids, are involved in de novo mutations that are markedly overrepresented in keratins. Hence, keratins have evolutionarily conserved and domain-selectively enriched amino acids including glycine and phenylalanine (epidermal), cysteine and proline (hair), and basic and acidic (simple-type epithelial), which reflect unique functions related to structural flexibility, rigidity and solubility, respectively. Our findings also support the importance of human keratin 'mutation hotspot' residues and their wild-type counterparts.
Authors:
Pavel Strnad; Valentyn Usachov; Cedric Debes; Frauke Gräter; David A D Parry; M Bishr Omary
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-01-03
Journal Detail:
Title:  Journal of cell science     Volume:  124     ISSN:  1477-9137     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2011 Dec 
Date Detail:
Created Date:  2012-01-16     Completed Date:  2012-07-03     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  4221-32     Citation Subset:  IM    
Affiliation:
Department of Internal Medicine I, Center for Internal Medicine, University Medical Center Ulm, Albert-Einstein-Allee 23, D-89081 Ulm, Germany. pavel.strnad@uniklinik-ulm.de
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis*
Animals
Cattle
Epidermis / chemistry
Evolution, Molecular
Humans
Keratins / chemistry*,  classification
Keratins, Hair-Specific / chemistry*
Mice
Protein Structure, Tertiary
Sequence Analysis, Protein
Grant Support
ID/Acronym/Agency:
DK47918/DK/NIDDK NIH HHS; DK52951/DK/NIDDK NIH HHS; R01 DK047918/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Keratins, Hair-Specific; 68238-35-7/Keratins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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