Evolution of Chitin-Binding Proteins in Invertebrates

Abstract

Analysis of a group of invertebrate proteins, including chitinases and peritrophic matrix proteins, reveals the presence of chitin-binding domains that share significant amino acid sequence similarity. The data suggest that these domains evolved from a common ancestor which may be a protein containing a single chitin-binding domain. The duplication and transposition of this chitin-binding domain may have contributed to the functional diversification of chitin-binding proteins. Sequence comparisons indicated that invertebrate and plant chitin binding domains do not share significant amino acid sequence similarity, suggesting that they are not coancestral. However, both the invertebrate and the plant chitin-binding domains are cysteine-rich and have several highly conserved aromatic residues. In plants, cysteines have been elucidated in maintaining protein folding and aromatic amino acids in interacting with saccharides [Wright HT, Sanddrasegaram G, Wright CS (1991) J Mol Evol 33:283-294]. It is likely that these residues perform similar functions in invertebrates. We propose that the invertebrate and the plant chitin-binding domains share similar mechanisms for folding and saccharide binding and that they evolved by convergent evolution. Furthermore, we propose that the disulfide bonds and aromatic residues are hallmarks for saccharide-binding proteins.

Binding of the AVR4 Elicitor of Cladosporium fulvum to Chitotriose Units Is Facilitated by Positive Allosteric Protein-Protein Interactions

“…The addition of longer chitooligomers resulted, however, in substantial heat of binding (Table I). The binding curves obtained for (GlcNAc) 3 , (GlcNAc) 4 , and (GlcNAc) 5 could be fitted, assuming a onebinding site model (Fig. 1, A-C).…”

“…In higher organisms, two CBMs predominantly confer binding of proteins to chitin, i.e. the Hevein domain (hereafter denoted as CBM18) (4) and the invertebrate chitin-binding domain (CBM14) (5). CBM18 is nearly exclusively found in plants (to date one additional member of CBM18 has been identified in Streptomyces griseus; Ref.…”

“…CBM18 is nearly exclusively found in plants (to date one additional member of CBM18 has been identified in Streptomyces griseus; Ref. 6), whereas CBM14 is commonly found in the genomes of baculoviridae, invertebrates, and mammals but absent in plants (5). Both ChBDs are typical CBMs, i.e.…”

A novel putative insect chitinase with multiple catalytic domains: hormonal regulation during metamorphosis

“…The intervening regions also contain four putative chitin-binding domains, each approx. 50 amino acids long, which conform to the consensus CX "" CX & CX * CX "# CX ( C (one-letter code) [26]. Two serine\threonine-rich mucin domains have been also identified between units 2 and 3 [27].…”

Retroactive, a membrane‐anchored extracellular protein related to vertebrate snake neurotoxin‐like proteins, is required for cuticle organization in the larva of Drosophila melanogaster

“…4A). It is important to note that Rtv does not contain any known chitin binding do-main or any other motif found in cuticle proteins (Andersen et al, 1995;Shen and Jacobs-Lorena, 1999;Suetake et al, 2000Suetake et al, , 2002 and, therefore, defines a new class of cuticle proteins.…”