A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle

Kosuke Fujita; Kumiko Shimomura; Kei ichiro Yamamoto; Tetsuro Yamashita; Koichi Suzuki

doi:10.1016/j.bbrc.2006.04.126

A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle

Kosuke Fujita, Kumiko Shimomura, Kei ichiro Yamamoto, Tetsuro Yamashita, Koichi Suzuki

Research output: Contribution to journal › Article › peer-review

49 Citations (Scopus)

Abstract

Two proteins (APAP I and II) of the glycoside hydrolase family 48 (Family GH48) were isolated from the active adults of the leaf beetle Gastrophysa atrocyanea. Full-length and cDNAs were sequenced. APAP I expression and function were examined in detail. The protein has a chitinase but not a glucanase and cellobiohydrolase activity. It is expressed in the feeding stages, including beetles whose diapause was terminated with a juvenile hormone agonist. Suppression of the APAP I expression by means of RNA interference prevented the hormonal termination of diapause.

Original language	English
Pages (from-to)	502-507
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	345
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2006.04.126
Publication status	Published - 2006 Jun 23
Externally published	Yes

Keywords

Chitinase
Feeding behavior
GH48
Glycoside hydrolase
Insect reproductive diapause

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/j.bbrc.2006.04.126

Cite this

A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle. / Fujita, Kosuke; Shimomura, Kumiko; Yamamoto, Kei ichiro et al.

In: Biochemical and biophysical research communications, Vol. 345, No. 1, 23.06.2006, p. 502-507.

Research output: Contribution to journal › Article › peer-review

@article{98497e7f7a33432d9436e8c924b3bc5c,

title = "A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle",

abstract = "Two proteins (APAP I and II) of the glycoside hydrolase family 48 (Family GH48) were isolated from the active adults of the leaf beetle Gastrophysa atrocyanea. Full-length and cDNAs were sequenced. APAP I expression and function were examined in detail. The protein has a chitinase but not a glucanase and cellobiohydrolase activity. It is expressed in the feeding stages, including beetles whose diapause was terminated with a juvenile hormone agonist. Suppression of the APAP I expression by means of RNA interference prevented the hormonal termination of diapause.",

keywords = "Chitinase, Feeding behavior, GH48, Glycoside hydrolase, Insect reproductive diapause",

author = "Kosuke Fujita and Kumiko Shimomura and Yamamoto, {Kei ichiro} and Tetsuro Yamashita and Koichi Suzuki",

note = "Funding Information: This study was supported in part by a Grant-in-Aid for JSPS Fellows (No. 16 5403, 2004) and a Grant-in-Aid for the 21st Century Center of Excellence Program (COE) from the Ministry of Education, Culture, Sports, Science and Technology of Japan. ",

year = "2006",

month = jun,

day = "23",

doi = "10.1016/j.bbrc.2006.04.126",

language = "English",

volume = "345",

pages = "502--507",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle

AU - Fujita, Kosuke

AU - Shimomura, Kumiko

AU - Yamamoto, Kei ichiro

AU - Yamashita, Tetsuro

AU - Suzuki, Koichi

N1 - Funding Information: This study was supported in part by a Grant-in-Aid for JSPS Fellows (No. 16 5403, 2004) and a Grant-in-Aid for the 21st Century Center of Excellence Program (COE) from the Ministry of Education, Culture, Sports, Science and Technology of Japan.

PY - 2006/6/23

Y1 - 2006/6/23

N2 - Two proteins (APAP I and II) of the glycoside hydrolase family 48 (Family GH48) were isolated from the active adults of the leaf beetle Gastrophysa atrocyanea. Full-length and cDNAs were sequenced. APAP I expression and function were examined in detail. The protein has a chitinase but not a glucanase and cellobiohydrolase activity. It is expressed in the feeding stages, including beetles whose diapause was terminated with a juvenile hormone agonist. Suppression of the APAP I expression by means of RNA interference prevented the hormonal termination of diapause.

AB - Two proteins (APAP I and II) of the glycoside hydrolase family 48 (Family GH48) were isolated from the active adults of the leaf beetle Gastrophysa atrocyanea. Full-length and cDNAs were sequenced. APAP I expression and function were examined in detail. The protein has a chitinase but not a glucanase and cellobiohydrolase activity. It is expressed in the feeding stages, including beetles whose diapause was terminated with a juvenile hormone agonist. Suppression of the APAP I expression by means of RNA interference prevented the hormonal termination of diapause.

KW - Chitinase

KW - Feeding behavior

KW - GH48

KW - Glycoside hydrolase

KW - Insect reproductive diapause

UR - http://www.scopus.com/inward/record.url?scp=33646395141&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33646395141&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2006.04.126

DO - 10.1016/j.bbrc.2006.04.126

M3 - Article

C2 - 16684504

AN - SCOPUS:33646395141

VL - 345

SP - 502

EP - 507

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -

A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this