Homology between cellulase genes of Trichoderma reesei

complete nucleotide sequence of the endoglucanase I gene

Merja Penttilä, Päivi Lehtovaara, Helena Nevalainen, Ramagauri Bhikhabhai, Jonathan Knowles

Research output: Contribution to journalArticleScientificpeer-review

249 Citations (Scopus)

Abstract

The filamentous fungus Trichoderma reesei produces several endoglucanases (EG) and cellobiohydrolases (CBH) which are involved in cellulose hydrolysis in a complex synergistic manner. We have cloned and sequenced the gene and the full-length cDNA coding for the major endoglucanase EG-I, and compared this to the cbhl gene sequence to clarify the relationship between the EG and CBH classes of cellulases. The deduced 437-amino acids (aa) long EG-I protein with a 22-aa long signal peptide is 45% identical in aa sequence with CBH-I. The best conserved region is found at the C terminus and shows about 70% homology. The data suggest that the two enzymes have arisen from a common ancestor by gene duplication. Despite this, the intron positions have not been conserved in these genes which both contain two short introns. The deduced EG-I sequence contains six putative N-glycosylation sites, and a putative O-glycosylated region is found near the C terminus, closely resembling a similar region at the C terminus of CBH-I. Comparison of the aa sequences suggests that the evolutionary divergence of EG-I from CBH-I has involved four separate 10-20 aa "deletions" from the ancestral protein.

Original languageEnglish
Pages (from-to)253-263
Number of pages11
JournalGene
Volume45
Issue number3
DOIs
Publication statusPublished - 1 Jan 1986
MoE publication typeA1 Journal article-refereed

Fingerprint

Cellulose 1,4-beta-Cellobiosidase
Cellulases
Trichoderma
Cellulase
Genes
Amino Acids
Introns
Amino Acid Sequence
Gene Duplication
Protein Sorting Signals
Glycosylation
Cellulose
Proteins
Hydrolysis
Fungi
Complementary DNA
Enzymes

Keywords

  • cDNA
  • cellobiohydrolase
  • filamentous fungus
  • gene family
  • glycosylation
  • introns
  • phage λ clones
  • Recombinant DNA

Cite this

Penttilä, Merja ; Lehtovaara, Päivi ; Nevalainen, Helena ; Bhikhabhai, Ramagauri ; Knowles, Jonathan. / Homology between cellulase genes of Trichoderma reesei : complete nucleotide sequence of the endoglucanase I gene. In: Gene. 1986 ; Vol. 45, No. 3. pp. 253-263.
@article{e699f6925c414312bc9c40f995c4293d,
title = "Homology between cellulase genes of Trichoderma reesei: complete nucleotide sequence of the endoglucanase I gene",
abstract = "The filamentous fungus Trichoderma reesei produces several endoglucanases (EG) and cellobiohydrolases (CBH) which are involved in cellulose hydrolysis in a complex synergistic manner. We have cloned and sequenced the gene and the full-length cDNA coding for the major endoglucanase EG-I, and compared this to the cbhl gene sequence to clarify the relationship between the EG and CBH classes of cellulases. The deduced 437-amino acids (aa) long EG-I protein with a 22-aa long signal peptide is 45{\%} identical in aa sequence with CBH-I. The best conserved region is found at the C terminus and shows about 70{\%} homology. The data suggest that the two enzymes have arisen from a common ancestor by gene duplication. Despite this, the intron positions have not been conserved in these genes which both contain two short introns. The deduced EG-I sequence contains six putative N-glycosylation sites, and a putative O-glycosylated region is found near the C terminus, closely resembling a similar region at the C terminus of CBH-I. Comparison of the aa sequences suggests that the evolutionary divergence of EG-I from CBH-I has involved four separate 10-20 aa {"}deletions{"} from the ancestral protein.",
keywords = "cDNA, cellobiohydrolase, filamentous fungus, gene family, glycosylation, introns, phage λ clones, Recombinant DNA",
author = "Merja Penttil{\"a} and P{\"a}ivi Lehtovaara and Helena Nevalainen and Ramagauri Bhikhabhai and Jonathan Knowles",
year = "1986",
month = "1",
day = "1",
doi = "10.1016/0378-1119(86)90023-5",
language = "English",
volume = "45",
pages = "253--263",
journal = "Gene",
issn = "0378-1119",
publisher = "Elsevier",
number = "3",

}

Homology between cellulase genes of Trichoderma reesei : complete nucleotide sequence of the endoglucanase I gene. / Penttilä, Merja; Lehtovaara, Päivi; Nevalainen, Helena; Bhikhabhai, Ramagauri; Knowles, Jonathan.

In: Gene, Vol. 45, No. 3, 01.01.1986, p. 253-263.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Homology between cellulase genes of Trichoderma reesei

T2 - complete nucleotide sequence of the endoglucanase I gene

AU - Penttilä, Merja

AU - Lehtovaara, Päivi

AU - Nevalainen, Helena

AU - Bhikhabhai, Ramagauri

AU - Knowles, Jonathan

PY - 1986/1/1

Y1 - 1986/1/1

N2 - The filamentous fungus Trichoderma reesei produces several endoglucanases (EG) and cellobiohydrolases (CBH) which are involved in cellulose hydrolysis in a complex synergistic manner. We have cloned and sequenced the gene and the full-length cDNA coding for the major endoglucanase EG-I, and compared this to the cbhl gene sequence to clarify the relationship between the EG and CBH classes of cellulases. The deduced 437-amino acids (aa) long EG-I protein with a 22-aa long signal peptide is 45% identical in aa sequence with CBH-I. The best conserved region is found at the C terminus and shows about 70% homology. The data suggest that the two enzymes have arisen from a common ancestor by gene duplication. Despite this, the intron positions have not been conserved in these genes which both contain two short introns. The deduced EG-I sequence contains six putative N-glycosylation sites, and a putative O-glycosylated region is found near the C terminus, closely resembling a similar region at the C terminus of CBH-I. Comparison of the aa sequences suggests that the evolutionary divergence of EG-I from CBH-I has involved four separate 10-20 aa "deletions" from the ancestral protein.

AB - The filamentous fungus Trichoderma reesei produces several endoglucanases (EG) and cellobiohydrolases (CBH) which are involved in cellulose hydrolysis in a complex synergistic manner. We have cloned and sequenced the gene and the full-length cDNA coding for the major endoglucanase EG-I, and compared this to the cbhl gene sequence to clarify the relationship between the EG and CBH classes of cellulases. The deduced 437-amino acids (aa) long EG-I protein with a 22-aa long signal peptide is 45% identical in aa sequence with CBH-I. The best conserved region is found at the C terminus and shows about 70% homology. The data suggest that the two enzymes have arisen from a common ancestor by gene duplication. Despite this, the intron positions have not been conserved in these genes which both contain two short introns. The deduced EG-I sequence contains six putative N-glycosylation sites, and a putative O-glycosylated region is found near the C terminus, closely resembling a similar region at the C terminus of CBH-I. Comparison of the aa sequences suggests that the evolutionary divergence of EG-I from CBH-I has involved four separate 10-20 aa "deletions" from the ancestral protein.

KW - cDNA

KW - cellobiohydrolase

KW - filamentous fungus

KW - gene family

KW - glycosylation

KW - introns

KW - phage λ clones

KW - Recombinant DNA

UR - http://www.scopus.com/inward/record.url?scp=0022969096&partnerID=8YFLogxK

U2 - 10.1016/0378-1119(86)90023-5

DO - 10.1016/0378-1119(86)90023-5

M3 - Article

VL - 45

SP - 253

EP - 263

JO - Gene

JF - Gene

SN - 0378-1119

IS - 3

ER -