Homologous domain in Trichoderma reesei cellulolytic enzymes

Gene sequence and expression of cellobiohydrolase II

Tuula Teeri, Päivi Lehtovaara, Sakari Kauppinen, Irma Salovuori, Jonathan Knowles

Research output: Contribution to journalArticleScientificpeer-review

272 Citations (Scopus)

Abstract

Fungal cellobiohydrolases are unique enzymes capable of degrading highly ordered crystalline cellulose. We present here the isolation and complete sequence analysis of the chromosomal and cDNA copies of the structural gene (cbh2) coding for one of the major cellobiohydrolases (CBH II) of Trichoderma reesei. We also present data on expression of the cbh2 gene and show that the transcription start points of the cbh2 gene are heterogeneous and are located 32 to 52 bp downstream from a putative TATA box. The derived CBH II protein sequence is 471 amino acids long and the coding region is interrupted by three short introns. Most of the CBH II protein bears no apparent resemblance to CBH I and endoglucanase I. However, a short region of extensive homology is found in all Trichoderma cellulases characterized so far, suggesting that this region is important for cellulose hydrolysis. The implications of this information with regard to the evolution of fungal cellulase genes and the enzymology of cellulose hydrolysis are discussed.

Original languageEnglish
Pages (from-to)43-52
Number of pages10
JournalGene
Volume51
Issue number1
DOIs
Publication statusPublished - 1987
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Trichoderma
Cellulose
Cellulases
Gene Expression
Hydrolysis
Enzymes
Fungal Genes
TATA Box
Cellulase
Introns
Genes
Sequence Analysis
Proteins
Complementary DNA
Amino Acids

Cite this

Teeri, Tuula ; Lehtovaara, Päivi ; Kauppinen, Sakari ; Salovuori, Irma ; Knowles, Jonathan. / Homologous domain in Trichoderma reesei cellulolytic enzymes : Gene sequence and expression of cellobiohydrolase II. In: Gene. 1987 ; Vol. 51, No. 1. pp. 43-52.
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abstract = "Fungal cellobiohydrolases are unique enzymes capable of degrading highly ordered crystalline cellulose. We present here the isolation and complete sequence analysis of the chromosomal and cDNA copies of the structural gene (cbh2) coding for one of the major cellobiohydrolases (CBH II) of Trichoderma reesei. We also present data on expression of the cbh2 gene and show that the transcription start points of the cbh2 gene are heterogeneous and are located 32 to 52 bp downstream from a putative TATA box. The derived CBH II protein sequence is 471 amino acids long and the coding region is interrupted by three short introns. Most of the CBH II protein bears no apparent resemblance to CBH I and endoglucanase I. However, a short region of extensive homology is found in all Trichoderma cellulases characterized so far, suggesting that this region is important for cellulose hydrolysis. The implications of this information with regard to the evolution of fungal cellulase genes and the enzymology of cellulose hydrolysis are discussed.",
author = "Tuula Teeri and P{\"a}ivi Lehtovaara and Sakari Kauppinen and Irma Salovuori and Jonathan Knowles",
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Homologous domain in Trichoderma reesei cellulolytic enzymes : Gene sequence and expression of cellobiohydrolase II. / Teeri, Tuula; Lehtovaara, Päivi; Kauppinen, Sakari; Salovuori, Irma; Knowles, Jonathan.

In: Gene, Vol. 51, No. 1, 1987, p. 43-52.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Homologous domain in Trichoderma reesei cellulolytic enzymes

T2 - Gene sequence and expression of cellobiohydrolase II

AU - Teeri, Tuula

AU - Lehtovaara, Päivi

AU - Kauppinen, Sakari

AU - Salovuori, Irma

AU - Knowles, Jonathan

PY - 1987

Y1 - 1987

N2 - Fungal cellobiohydrolases are unique enzymes capable of degrading highly ordered crystalline cellulose. We present here the isolation and complete sequence analysis of the chromosomal and cDNA copies of the structural gene (cbh2) coding for one of the major cellobiohydrolases (CBH II) of Trichoderma reesei. We also present data on expression of the cbh2 gene and show that the transcription start points of the cbh2 gene are heterogeneous and are located 32 to 52 bp downstream from a putative TATA box. The derived CBH II protein sequence is 471 amino acids long and the coding region is interrupted by three short introns. Most of the CBH II protein bears no apparent resemblance to CBH I and endoglucanase I. However, a short region of extensive homology is found in all Trichoderma cellulases characterized so far, suggesting that this region is important for cellulose hydrolysis. The implications of this information with regard to the evolution of fungal cellulase genes and the enzymology of cellulose hydrolysis are discussed.

AB - Fungal cellobiohydrolases are unique enzymes capable of degrading highly ordered crystalline cellulose. We present here the isolation and complete sequence analysis of the chromosomal and cDNA copies of the structural gene (cbh2) coding for one of the major cellobiohydrolases (CBH II) of Trichoderma reesei. We also present data on expression of the cbh2 gene and show that the transcription start points of the cbh2 gene are heterogeneous and are located 32 to 52 bp downstream from a putative TATA box. The derived CBH II protein sequence is 471 amino acids long and the coding region is interrupted by three short introns. Most of the CBH II protein bears no apparent resemblance to CBH I and endoglucanase I. However, a short region of extensive homology is found in all Trichoderma cellulases characterized so far, suggesting that this region is important for cellulose hydrolysis. The implications of this information with regard to the evolution of fungal cellulase genes and the enzymology of cellulose hydrolysis are discussed.

U2 - 10.1016/0378-1119(87)90472-0

DO - 10.1016/0378-1119(87)90472-0

M3 - Article

VL - 51

SP - 43

EP - 52

JO - Gene

JF - Gene

SN - 0378-1119

IS - 1

ER -