Carbohydrate Binding Module Family 19 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:17:27Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Elizabeth Ficko-Blean at 15:26, 21 January 2021

2021-01-21T15:26:53Z

Elizabeth Ficko-Blean at 15:26, 21 January 2021

2021-01-21T15:26:24Z

Elizabeth Ficko-Blean at 15:25, 21 January 2021

2021-01-21T15:25:09Z

Elizabeth Ficko-Blean at 15:20, 21 January 2021

2021-01-21T15:20:50Z

Elizabeth Ficko-Blean at 14:54, 21 January 2021

2021-01-21T14:54:09Z

Elizabeth Ficko-Blean at 14:45, 21 January 2021

2021-01-21T14:45:32Z

Elizabeth Ficko-Blean at 14:40, 21 January 2021

2021-01-21T14:40:04Z

Elizabeth Ficko-Blean at 14:29, 21 January 2021

2021-01-21T14:29:56Z

Elizabeth Ficko-Blean at 12:52, 21 January 2021

2021-01-21T12:52:45Z

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 {{CuratorApproved}}
-* [[Author]]: ^^^Elizabeth Ficko-Blean^^^
+* [[Author]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
-* [[Responsible Curator]]:  ^^^Elizabeth Ficko-Blean^^^
+* [[Responsible Curator]]:  [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
 ----

← Older revision		Revision as of 15:26, 21 January 2021
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	There is no 3D structure available for the CBM19 family.		There is no 3D structure available for the CBM19 family.
−

	== Functionalities ==		== Functionalities ==

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
-{{UnderConstruction}}
+{{CuratorApproved}}
 * [[Author]]: ^^^Elizabeth Ficko-Blean^^^
 * [[Responsible Curator]]:  ^^^Elizabeth Ficko-Blean^^^
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 == Structural Features ==
-[[File:CST1.png|thumb|300px|right|'''Figure 1.'''  A primary structure representation of the ''S. cerevisiae'' CST1 protein (not to scale)<cite>Kuranda1991</cite>. The N and the C termini are annotated.  SP represents signal peptide, [[GH18]] is a family 18 glycoside hydrolase, S/T-rich is the serine/threonine rich heavily glycosylated region and CBM19 is the family 19 carbohydrate-binding module.]]
+[[File:CST1.png|thumb|300px|right|'''Figure 1.'''  A primary structure representation of the ''S. cerevisiae'' CST1 protein (not to scale)<cite>Kuranda1991</cite>. The N and the C termini are annotated.  SP represents signal peptide, [[GH18]] is a family 18 glycoside hydrolase, S/T rich is the serine/threonine-rich heavily glycosylated region and CBM19 is the family 19 carbohydrate-binding module.]]
 Two alleles of the ''cts1'' gene have been identified, they are referred to as ''cts1-1'' and ''cts1-2'' <cite>Kuranda1991</cite>.  The predicted full length protein is likely divided into four domains (Figure 1) <cite>Kuranda1991</cite>. The first domain (amino acids 1-20) is the cleavable signal sequence, the second domain is the chitinase [[GH18]] catalytic domain (amino acids 21-327), the third domain is a highly glycosylated serine/threonine-rich domain (amino acids 328-480) and the fourth domain is the chitin binding CBM19 <cite>Kuranda1991 Lombard2014</cite>.

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 == Ligand specificities ==
-The CBM19 found in the CTS1 chitinase produced by ''Saccharomyces cerevisiae'' has been characterized as a chitin-binding CBM <cite>Kuranda1991</cite>.  The authors produced several manipulated constructs in yeast to demonstrate chitin binding including making a C-terminal deletion mutant, controlled proteolysis of the wild-type enzyme, production of only the C-terminal CBM11 with the N-terminal signal sequence and fusion of the CBM19 with the yeast invertase SUC2 <cite>Kuranda1991</cite>. These different constructs were then tested for their chitin-binding capabilities. The CBM19 is suggested to bind with high affinity, though no binding affinity was experimentally determined <cite>Kuranda1991</cite>. Interestingly, the C-terminal deletion mutant showed an enhanced rate of chitin hydrolysis relative to the wild type.
+The CBM19 found in the CTS1 chitinase produced by ''Saccharomyces cerevisiae'' has been characterized as a chitin-binding CBM <cite>Kuranda1991</cite>.  The authors produced several manipulated constructs in yeast to demonstrate chitin binding including a C-terminal deletion mutant, controlled proteolysis of the wild-type enzyme, production of a fused N-terminal signal sequence directly to the C-terminal CBM19 and fusion of the CBM19 with the yeast invertase SUC2 <cite>Kuranda1991</cite>. These different constructs were then tested for their chitin-binding capabilities. The CBM19 is suggested to bind with high affinity, though no binding affinity was experimentally determined <cite>Kuranda1991</cite>. Interestingly, the C-terminal deletion mutant showed an enhanced rate of chitin hydrolysis relative to the wild type.
 == Structural Features ==
 [[File:CST1.png|thumb|300px|right|'''Figure 1.'''  A primary structure representation of the ''S. cerevisiae'' CST1 protein (not to scale)<cite>Kuranda1991</cite>. The N and the C termini are annotated.  SP represents signal peptide, [[GH18]] is a family 18 glycoside hydrolase, S/T-rich is the serine/threonine rich heavily glycosylated region and CBM19 is the family 19 carbohydrate-binding module.]]
-Two alleles of the ''cts1'' gene have been identified, they are referred to as ''cts1-1'' and ''cts1-2'' <cite>Kuranda1991</cite>.  The predicted full length protein is likely divided into four domains <cite>Kuranda1991</cite>. The first domain (amino acids 1-20) is the cleavable signal sequence, the second domain is the chitinase [[GH18]] catalytic domain (amino acids 21-327), the third domain is a highly glycosylated serine/threonine-rich domain (amino acids 328-480) and the fourth domain is the chitin binding CBM19 <cite>Kuranda1991 Lombard2014</cite>.
+Two alleles of the ''cts1'' gene have been identified, they are referred to as ''cts1-1'' and ''cts1-2'' <cite>Kuranda1991</cite>.  The predicted full length protein is likely divided into four domains (Figure 1) <cite>Kuranda1991</cite>. The first domain (amino acids 1-20) is the cleavable signal sequence, the second domain is the chitinase [[GH18]] catalytic domain (amino acids 21-327), the third domain is a highly glycosylated serine/threonine-rich domain (amino acids 328-480) and the fourth domain is the chitin binding CBM19 <cite>Kuranda1991 Lombard2014</cite>.
 There is no 3D structure available for the CBM19 family.
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 == Functionalities ==
-Chitin is an important component of the cell wall of ''Saccharomyces cerevisiae''.  It is specifically located at the junction of mother and daughter cells providing mechanical stability.  The CTS1 enzyme, containing a [[GH18]] catalytic module is produced by ''S. cerevisiae''  and hydrolyses chitin<cite>Correa1982 Kuranda1987</cite> and has a role in cell separation <cite>Kuranda1991</cite>. When chitinase activity was disrupted cells were unable to separate normally resulting in  aggregates of cells connected by their cell septum regions <cite>Kuranda1991</cite>. Complementation experiments were able to restore the separation phenotype with plasmids containing ''cts1-1'' or ''cts1-2''; however,  the C-terminal deletion mutant only partly restores the phenotype <cite>Kuranda1991</cite>.  This suggests the CBM19 is involved in the mechanism of cell separation between mother and daughter cells.
+Chitin is an important component of the cell wall of ''S. cerevisiae''.  It is specifically located at the junction of mother and daughter cells providing mechanical stability.  The CTS1 enzyme, containing a [[GH18]] catalytic module is produced by ''S. cerevisiae''  and hydrolyses chitin<cite>Correa1982 Kuranda1987</cite> and has a role in cell separation <cite>Kuranda1991</cite>. When chitinase activity was disrupted cells were unable to separate normally resulting in aggregates of cells connected by their cell septum regions <cite>Kuranda1991</cite>. Complementation experiments were able to restore the separation phenotype with plasmids containing ''cts1-1'' or ''cts1-2''; however,  the C-terminal deletion mutant only partly restores the phenotype <cite>Kuranda1991</cite>.  This suggests the CBM19 is involved in the mechanism of cell separation between mother and daughter cells.
 == Family Firsts ==

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 The CBM19 found in the CTS1 chitinase produced by ''Saccharomyces cerevisiae'' has been characterized as a chitin-binding CBM <cite>Kuranda1991</cite>.  The authors produced several manipulated constructs in yeast to demonstrate chitin binding including making a C-terminal deletion mutant, controlled proteolysis of the wild-type enzyme, production of only the C-terminal CBM11 with the N-terminal signal sequence and fusion of the CBM19 with the yeast invertase SUC2 <cite>Kuranda1991</cite>. These different constructs were then tested for their chitin-binding capabilities. The CBM19 is suggested to bind with high affinity, though no binding affinity was experimentally determined <cite>Kuranda1991</cite>. Interestingly, the C-terminal deletion mutant showed an enhanced rate of chitin hydrolysis relative to the wild type.
 Two alleles of the ''cts1'' gene have been identified, they are referred to as ''cts1-1'' and ''cts1-2'' <cite>Kuranda1991</cite>.  The predicted full length protein is likely divided into four domains <cite>Kuranda1991</cite>. The first domain (amino acids 1-20) is the cleavable signal sequence, the second domain is the chitinase [[GH18]] catalytic domain (amino acids 21-327), the third domain is a highly glycosylated serine/threonine-rich domain (amino acids 328-480) and the fourth domain is the chitin binding CBM19 <cite>Kuranda1991 Lombard2014</cite>.
 There is no 3D structure available for the CBM19 family.
 == Functionalities ==

← Older revision		Revision as of 14:40, 21 January 2021
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	== Functionalities ==		== Functionalities ==
−	Chitin is an important component of the cell wall of ''Saccharomyces cerevisiae''. It is specifically located at the junction of mother and daughter cells providing mechanical stability. The CTS1 enzyme produced by ''S. cerevisiae'' hydrolyses chitin <cite>Correa1982 Kuranda1987</cite> and has a role in cell separation <cite>Kuranda1991</cite>.	+	Chitin is an important component of the cell wall of ''Saccharomyces cerevisiae''. It is specifically located at the junction of mother and daughter cells providing mechanical stability. The CTS1 enzyme produced by ''S. cerevisiae'' hydrolyses chitin <cite>Correa1982 Kuranda1987</cite> and has a role in cell separation <cite>Kuranda1991</cite>. When chitinase activity was disrupted cells were unable to separate normally resulting in aggregates of cells connected by their cell septum regions <cite>Kuranda1991</cite>.