CLONING AND EXPRESSION OF CHITINASE 19 FAMILIE FROM D.CAPENSIS

2020 ◽  
pp. 288-290
Author(s):  
A. Chulkin ◽  
A. Rozhkova ◽  
A. Sinitsyn A.
Keyword(s):  
Binding Domain ◽  
Full Length ◽  
Cloning And Expression ◽  
Chitin Binding Domain ◽  
Biochemical Characteristics ◽  
Family 19 Chitinase ◽  
Different Strains

Sequence of family 19 chitinase was cloned from Drosera capensis. Implemented expression in different strains of E.coli and developed a refolding method. Describes the primary biochemical characteristics of the full-length chitinase and its shape without chitin-binding domain.

scholarly journals X-Ray Crystal Structure of the Full Length Human Chitotriosidase (CHIT1) Reveals Features of Its Chitin Binding Domain

PLoS ONE ◽  
2016 ◽  
Vol 11 (4) ◽  
pp. e0154190 ◽  
Author(s):  
Firas Fadel ◽  
Yuguang Zhao ◽  
Alexandra Cousido-Siah ◽  
Francesc X. Ruiz ◽  
André Mitschler ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Domain ◽  
Full Length ◽  
Chitin Binding Domain ◽  
X Ray

scholarly journals Microtubule Actin Cross-Linking Factor (Macf)

1999 ◽  
Vol 147 (6) ◽  
pp. 1275-1286 ◽  
Author(s):  
Conrad L. Leung ◽  
Dongming Sun ◽  
Min Zheng ◽  
David R. Knowles ◽  
Ronald K.H. Liem
Keyword(s):  
Calcium Binding ◽  
Coiled Coil ◽  
Specific Protein ◽  
Binding Domain ◽  
Full Length ◽  
Actin Binding ◽  
Cross Linking ◽  
Actin Binding Domain

We cloned and characterized a full-length cDNA of mouse actin cross-linking family 7 (mACF7) by sequential rapid amplification of cDNA ends–PCR. The completed mACF7 cDNA is 17 kb and codes for a 608-kD protein. The closest relative of mACF7 is the Drosophila protein Kakapo, which shares similar architecture with mACF7. mACF7 contains a putative actin-binding domain and a plakin-like domain that are highly homologous to dystonin (BPAG1-n) at its NH2 terminus. However, unlike dystonin, mACF7 does not contain a coiled–coil rod domain; instead, the rod domain of mACF7 is made up of 23 dystrophin-like spectrin repeats. At its COOH terminus, mACF7 contains two putative EF-hand calcium-binding motifs and a segment homologous to the growth arrest–specific protein, Gas2. In this paper, we demonstrate that the NH2-terminal actin-binding domain of mACF7 is functional both in vivo and in vitro. More importantly, we found that the COOH-terminal domain of mACF7 interacts with and stabilizes microtubules. In transfected cells full-length mACF7 can associate not only with actin but also with microtubules. Hence, we suggest a modified name: MACF (microtubule actin cross-linking factor). The properties of MACF are consistent with the observation that mutations in kakapo cause disorganization of microtubules in epidermal muscle attachment cells and some sensory neurons.

Tight attachment of chitin-binding-domain-tagged proteins to surfaces coated with acetylated chitosan

2004 ◽  
Vol 327 (2) ◽  
pp. 278-283 ◽  
Author(s):  
Michael P Bernard ◽  
Donghui Cao ◽  
Rebecca V Myers ◽  
William R Moyle
Keyword(s):  
Binding Domain ◽  
Chitin Binding Domain
Sign in / Sign up

Export Citation Format

Share Document