UNIVERSIDAD NACIONAL DE TUMBES

FACULTAD DE CIENCIAS AGRARIAS

ESCUELA PROFESIONAL DE INGENIERÍA FORESTAL Y MEDIO
AMBIENTE

TEMA:

Conectores lógicos.

Asignatura:

Genética.

DOCENTE:

Msc. Suarez Peña, Erick Antonio.

CICLO:

IV

ESTUDIANTE:

Alemán Navarro, Johana.

TUMBES- PERÚ
2023
84
Curr Genet (1994) 27: 83-89
Irene García • José M. Lora • Jesús de la Cruz
Tahía Benítez Antonio Llobell • José A. Pintor-Toro
Cloning and characterization of a chitinase (CHIT42) cDNA
from the mycoparasitic fungus Trichoderma harzianum
Received: 5 April 1994
Abstract A cDNA of Trichoderma harzianum (chit42),
coding for an endochitinase of 42 kDa, has been
cloned using synthetic oligonucleotides corresponding
to aminoacid sequences of the purified chitinase. The
cDNA codes for a protein of 423 amino acids.
Analysis of the N-terminal amino-acid sequence of the
chitinase, and comparison with that deduced from the
nucleotide sequence, revealed post-translational
processing of a putative signal peptide of 22 amino
acids and a second peptide of 12 amino acids. The
chit42 sequence presents overall similarities with
filamentous fungal and bacterial chitinases and to a
lesser extent with yeast and plant chitinases. The
deduced aminoacid sequence has putative catalytic,
phosphorylation and glycosylation domains.
Expression of chit42 mRNA is strongly induced by
chitin and chitin-containing cell walls and is subjected
to catabolite repression. Southern analysis shows that
it is present as a single-copy gene in T. harzianum.
chit42 is also detected in several tested mycoparasitic
and non-mycoparasitic fungal strains.
Key words Trichoderma • Chitinase • Mycoparasitism
Biological control
Introduction
Chitinases (E.C. 3.2.1.14) are enzymes that
endolytically hydrolyze the ß-l ,4-linkage of chitin, a
structural polymer
1. García J. M. Lora • J. A. Pintor-Toro (E) Instituto
de Recursos Naturales y Agrobiología,
CSIC, Apdo., E-1052, Sevilla, Spain
J. de la Cruz • A. Llobell
Instituto de Bioquímica Vegetal y Fotosíntesis,
CSIC and Universidad de Sevilla,
Apdo. E-1113, Sevilla, Spain
© Springer-Verlag 1994
T. Benítez
Departamento de Genética, Universidad de Sevilla, Apdo.,
E-1095, Sevilla, Spain
Communicated by B. S. Lox
of many arthropods and fungi (Cabib 1987). These enzymes
are widely distributed in nature and can play many different
roles (Chen et al. 1982; Jones et al. 1986). Their
physiological function in plants is not known since the
substrate. chitin, is not present. However, chitin and p- I ,3-
glucans are major components of many fungal cell walls
(Bartnicki-García 1968), and, therefore, it has been proposed
that chitinases are involved in protecting plants against
fungal pathogens (Collinge et al. 1993). In fungi, chitinases
seem to play a morphogenetic role during apical growth, cell
division and differentiation, as well as a nutritional role
related to those species saprophytic and mycoparasitic in
fungi (Papavizas 1985; Cabib 1987; Kuranda and Robbins
1991).
Soil-borne fungi of the genus Trichoderma have been
described as the best-known biological control agents
against fungal plant pathogens (Papavizas 1985). The
degradation and further assimilation of the phytopathogenic
fungi, namely mycoparasitism, has been proposed as the
major mechanism accounting for their antagonistic action.
Chitinases and P-1,3-glucanases have been suggested as the
key enzymes involved in this process (Chérif and Benhamon
1990; Elad et al. 1982; Ridout et al. 1986). Some
controversial experimental results have also been reported
with regard to the potential role attributed to chitinases,
since no correlation was found between antagonism against
Rhizoctonia solani and the hydrolytic activity of
Trichoderma spp. (Kohl and Schlosser 1992). Moreover.
mutants of Gliocadium virens deficient in mycoparasitic
ability were still capable of controlling R. solani (Howell
1987). Additionally, it has been proposed that the
breakdown of fungal hyphae is due to a nutrient stress
caused by the mycoparasite (Adams 1990).
Due to the interest generated by the role of chitinase, a
great number of chitinase genes have been isolated and
analyzed in recent years. Chitinase-encoding genes have
been