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. 2001 Jul;6(3):219-24.
doi: 10.1379/1466-1268(2001)006<0219:athpka>2.0.co;2.

Arabidopsis thaliana Hsp100 proteins: kith and kin

M Agarwal  1 , S Katiyar-Agarwal, C Sahi, D R Gallie, A Grover
Affiliations

Arabidopsis thaliana Hsp100 proteins: kith and kin

M Agarwal et al. Cell Stress Chaperones. 2001 Jul.

Abstract

Arabidopsis thaliana, the first plant for which the entire genome sequence is available, was also among the first plant species from which Hsp100 proteins were characterized. The Athsp101 complementary DNA (cDNA) corresponds to the gene identification At1g74310 in the Arabidopsis genome sequence. Analysis of the genome revealed 7 additional proteins that are variably homologous with At1g74310 throughout the entire amino acid sequence and significant similarities or identities in the signature sequences conserved among Hsp100 proteins. Although AtHsp101 is cytoplasmic, 5 of the 7 related proteins have predicted plastidial localization signals. This complete description of the AtHsp100 family sets the stage for future research on expression and function.

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Figures

Fig 1.
Fig 1.
Block diagrams of AtHsp100 and its homologues. Arrowheads show the positions of introns. Numbers given on top represent the length of a given domain (number of amino acid residues). The color code and pictographs are explained at the bottom (see text and Figs 3 and 4 for further details)
Fig 2.
Fig 2.
Phylogenetic relationships among Arabidopsis Hsp100 and related proteins. The scale bar shows the correspondence between the unit length and the number of substitution events per position. The phylogenetic tree was constructed using the J. Hein method with residue weight set at PAM 250 in the Megalign program of DNaStar
Fig 3.
Fig 3.
Sequence alignments of the signature sequences present in NBD1 and spacer domain of Arabidopsis Hsp100 and related protein members. The consensus sequences described by Schirmer et al (1996) are indicated at the top of the boxes. Large case letters represent the corresponding amino acid residues in the 1-letter code; x is any amino acid residue, whereas h stands for any of the hydrophobic amino acid residues, ie, isoleucine, leucine, valine, methionine, phenylalanine, or tyrosine. Note that in some cases these consensus motifs do not reflect the reality of the Arabidopsis Hsp100 proteins (see examples of signature sequence II and Walker B motif in NBD2)
Fig 4.
Fig 4.
Sequence alignments of the signature sequences present in NBD2 and C-terminal domain of Arabidopsis Hsp100 and related protein members. For further explanations see legend to Fig 3
See this image and copyright information in PMC

References

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