A Grover

A Kasprzewska

A Nakatsuka

A Schlumbaum

A Singh

A Vitale

B Halliwell

B Henrissat

B Iseli

C Akimoto

C Carter

CH Park

D Liu

D Nocentini

DB Collinge

DF Chamberlain

E Gasteiger

E Pacini

F Brunner

F Hamel

G Jach

H Eilenberg

H Schagger

Hang Sun

HG Baker

HG Zha

Hong-Guang Zha

Hong-Xia Zhou

I Dore

J Flach

J Huet

J Trudel

JD Evans

JJ Beintema

JM Neuhaus

K Broglie

K Lawton

KH Oldach

KLB Chang

L Jaakola

LS Melchers

M Dubois

M Esaka

M Escalante-Perez

M Ferrari

M Gonzalez-Teuber

M Heil

MA Larkin

ME Alvarez

MM Bradford

MS Hillwig

N Benhamou

N Kobayashi

NA Udaya Prakash

O Emanuelsson

OE Prŷs-Jones

PC Molan

PJ Seo

R Hamid

R Wagner

RB Primack

Richard I. Milne

RJ Weston

S Adrangi

S Briesemeister

S Chamnongpol

S Nicolson

T Kikuchi

TN Petersen

UK Laemmli

W Lin

Xiang-Yang Chen

Y Peng

Y Takenaka

YG Liu

Z Minic

Class II and III chitinases belonging to different glycoside hydrolase families were major nectarins in Rhododendron irroratum floral nectar which showed significant chitinolytic activity. Previous studies have demonstrated antimicrobial activity in plant floral nectar, but the molecular basis for the mechanism is still poorly understood. Two chitinases, class II (Rhchi2) and III (Rhchi3), were characterized from alkaline Rhododendron irroratum nectar by both SDS-PAGE and mass spectrometry. Rhchi2 (27 kDa) and Rhchi3 (29 kDa) are glycoside hydrolases (family 19 and 18) with theoretical pI of 8.19 and 7.04. The expression patterns of Rhchi2 and Rhchi3 were analyzed by semi-quantitative RT-PCR. Rhchi2 is expressed in flowers (corolla nectar pouches) and leaves while Rhchi3 is expressed in flowers. Chitinase in concentrated protein and fresh nectar samples was visualised by SDS-PAGE and chitinolytic activity in fresh nectar was determined spectrophotometrically via chitinazure. Full length gene sequences were cloned with Tail-PCR and RACE. The amino acid sequence deduced from the coding region for these proteins showed high identity with known chitinases and predicted to be located in extracellular space. Fresh R. irroratum floral nectar showed significant chitinolytic activity. Our results demonstrate that class III chitinase (GH 18 family) also exists in floral nectar. The functional relationship between class II and III chitinases and the role of these pathogenesis-related proteins in antimicrobial activity in nectar is suggested

Zha, Hong-guang

Milne, Richard I.

Zhou, Hong-xia

Chen, Xiang-yang

Sun, Hang

Edinburgh Research Explorer

Identification and cloning of class II and III chitinases from alkaline floral nectar of Rhododendron irroratum, Ericaceae

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https://www.pure.ed.ac.uk/ws/files/25304152/Identification_and_cloning_of_class_II_and_III_chitinases_from_alkaline.....pdf

Identification and cloning of class II and III chitinases from alkaline floral nectar of Rhododendron irroratum, Ericaceae

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