Cellulosome - Revision history

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

2021-12-18T21:15:44Z

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

Bareket Dassa at 07:06, 23 June 2010

2010-06-23T07:06:19Z

Bareket Dassa at 07:05, 23 June 2010

2010-06-23T07:05:28Z

Bareket Dassa at 06:57, 23 June 2010

2010-06-23T06:57:35Z

Harry Brumer at 09:44, 21 June 2010

2010-06-21T09:44:40Z

Bareket Dassa at 08:31, 21 June 2010

2010-06-21T08:31:03Z

Bareket Dassa at 08:29, 21 June 2010

2010-06-21T08:29:30Z

Bareket Dassa at 11:10, 16 June 2010

2010-06-16T11:10:41Z

Bareket Dassa at 10:56, 16 June 2010

2010-06-16T10:56:03Z

Bareket Dassa at 08:37, 16 June 2010

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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]]s: ^^^Orly Alber^^^, ^^^Bareket Dassa^^^, and ^^^Ed Bayer^^^
+* [[Author]]s: [[User:Orly Alber|Orly Alber]], [[User:Bareket Dassa|Bareket Dassa]], and [[User:Ed Bayer|Ed Bayer]]
-* [[Responsible Curator]]:  ^^^Ed Bayer^^^
+* [[Responsible Curator]]:  [[User:Ed Bayer|Ed Bayer]]
 ----

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 #cellulosome6 pmid=15755956
 #cellulosome7 pmid=20070943
-#cellulosome8  pmid=3301817
+#cellulosome8 pmid=3301817
 #BayerLabEnzymesPage http://www.weizmann.ac.il/Biological_Chemistry/scientist/Bayer/new_pages/reserch_topics/enzymes.html Accessed 2010-05-28
 #BayerLabCellulosomeSystemsPage http://www.weizmann.ac.il/Biological_Chemistry/scientist/Bayer/new_pages/reserch_topics/cellulosome_systems.html Accessed 2010-05-28.

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 == Cellulosome complex ==
-Cellulosome complexes are intricate multi-enzyme machines produced by many cellulolytic microorganisms. They are designed for efficient degradation of plant cell wall polysaccharides, notably cellulose — the most abundant organic polymer on Earth. The cellulosome consists of a multi-functional integrating subunit (called scaffoldin), responsible for organizing the various cellulolytic subunits (e.g., the enzymes) into the complex. Within a cellulosome, multiple endoglucanases, cellobiohydrolases, xylanases and other degradative enzymes work synergistically to attack heterogeneous, insoluble cellulose substrates. This is accomplished by the interaction of two complementary classes of module, located on the two separate types of interacting subunits, i.e., a cohesin module on the scaffoldin and a dockerin module on each enzymatic subunit. The high-affinity cohesin-dockerin interaction defines the cellulosome structure. Attachment of the cellulosome to its substrate is mediated by a scaffoldin-borne cellulose-binding module (CBM) that comprises part of the scaffoldin subunit.  Much of our understanding of its catalytic components, architecture, and mechanisms of attachment to the bacterial cell and to cellulose, has been derived from the study of ''Clostridium thermocellum''.
+Cellulosome complexes are intricate multi-enzyme machines produced by many cellulolytic microorganisms. They are designed for efficient degradation of plant cell wall polysaccharides, notably cellulose — the most abundant organic polymer on Earth. The cellulosome consists of a multi-functional integrating subunit (called scaffoldin), responsible for organizing the various cellulolytic subunits (e.g., the enzymes) into the complex. Within a cellulosome, multiple endoglucanases, cellobiohydrolases, xylanases and other degradative enzymes work synergistically to attack heterogeneous, insoluble cellulose substrates. This is accomplished by the interaction of two complementary classes of module, located on the two separate types of interacting subunits, i.e., a cohesin module on the scaffoldin and a dockerin module on each enzymatic subunit. The high-affinity cohesin-dockerin interaction defines the cellulosome structure. Attachment of the cellulosome to its substrate is mediated by a scaffoldin-borne cellulose-binding module (CBM) that comprises part of the scaffoldin subunit.  Much of our understanding of its catalytic components, architecture, and mechanisms of attachment to the bacterial cell and to cellulose, has been derived from the study of ''Clostridium thermocellum'' <cite>cellulosome1 cellulosome2 cellulosome3 cellulosome5</cite>.
 [[File:Cellulosome.jpg|500px|thumb|Architecture of the ''C. thermocellum'' cellulosome system]]
 '''Cellulosome components:'''

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 * Crystal structure of cellulosomal enzyme <cite>2</cite>
 * Functional role of dockerin module (duplicated domain) <cite>Firsts11</cite>
-* Sequencing and characterization of primary scaffoldin genes <cite>Firsts13 Firsts14</cite>
+* Sequencing and characterization of primary scaffoldin genes <cite>species6 Firsts14</cite>
 * Sequencing of cell-surface anchoring scaffoldins <cite>Firsts15</cite>
-* Definition of “cohesin”, “dockerin” and “scaffoldin” <cite>Firsts16</cite>
+* Definition of “cohesin”, “dockerin” and “scaffoldin” <cite>Firsts2</cite>
 * Functional role of cohesins <cite>Firsts1</cite>
-* Establishment of designer cellulosome concept <cite>Firsts3 Firsts1 Firsts16</cite>
+* Establishment of designer cellulosome concept <cite>Firsts3 Firsts1 Firsts2</cite>
 * Crystal structures of cohesins and cohesin-dockerin complexes <cite>Firsts6 Firsts5 Firsts4 Firsts3</cite>
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 #Firsts11 pmid=1936262
 #Firsts12 pmid=3301817
 #Firsts14 pmid=8316083
 #Firsts15 pmid=8458832
 #1 Lamed et al., Enzyme Microb Technol 1985;7:37-41, 1985

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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]]s: ^^^Orly Alber^^^, ^^^Bareket Dassa^^^, and ^^^Ed Bayer^^^

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 ==  Cellulosome Firsts  ==
 * Discovery of the cellulosome in ''Clostridium thermocellum'' <cite>Firsts7 Firsts8</cite>
-* Demonstration of true cellulase activity by the cellulosome (Lamed et al., Enzyme Microb Technol 1985;7:37-41, 1985)
+* Demonstration of true cellulase activity by the cellulosome <cite>1</cite>
 * Detailed ultrastructural characterization of the cellulosome <cite>Firsts9 Firsts10</cite>
 * Demonstration of the cellulosome-like entities in other cellulose-degrading strains <cite>Firsts12</cite>
-* Crystal structure of cellulosomal enzyme (Juy et al.,Nature 1992;357:39-41, 1992)
+* Crystal structure of cellulosomal enzyme <cite>2</cite>
 * Functional role of dockerin module (duplicated domain) <cite>Firsts11</cite>
 * Sequencing and characterization of primary scaffoldin genes <cite>Firsts13 Firsts14</cite>
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 #Firsts15 pmid=8458832
 #Firsts16 pmid=7765191
 </biblio>

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 * ''Clostridium thermocellum'' <cite>species9</cite>
 * ''Ruminococcus albus'' (dockerins identified, cohesins as yet undetected) <cite>species10</cite>
-* ''Ruminococcus flavifaciens'' <cite>species11 species12</cite>
+* ''Ruminococcus flavefaciens'' <cite>species11 species12</cite>
 Cellulosomes exist as extracellular complexes that are either attached to the cell wall of bacteria or free in solution, where the insoluble substrate can be broken down into soluble products and taken up by the cell. The large size and heterogeneity of cellulosomes from the best-characterized organisms (i.e., ''C. thermocellum'', ''C. cellulolyticum'', and ''C. cellulovorans'') have greatly complicated efforts to probe cellulosome structure and function. Other cellulosome systems (such as those from ''Acetivibrio cellulolyticus'' and ''Ruminococcus flavefaciens'') appear to be even more intricate.

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 * '''Dockerin modules''' anchor the catalytic enzymes to the scaffoldin. The dockerin displays internal two-fold symmetry, consisting of a duplicated F-hand motif (a calcium-binding loop preceding an a helix). The dockerin can also be found in the C- terminus of scaffoldins.
-* '''Catalytic subunits''' contain dockerin modules that serve to incorporate catalytic modules into the cellulosome complex. These catalytic modules include: [[glycoside hydrolases]], polysaccharide lyases, and carboxyl esterases '''Please cite a review or paper here''' (See also <cite>BayerLabEnzymesPage</cite>).
+* '''Catalytic subunits''' contain dockerin modules that serve to incorporate catalytic modules into the cellulosome complex. These catalytic modules include: [[glycoside hydrolases]], polysaccharide lyases, and carboxyl esterases (See also <cite>BayerLabEnzymesPage cellulosome4 cellulosome6</cite>).
 === Cellulosome systems ===
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 '''Complex Cellulosome Systems'''
-To date, complex cellulosome systems have been described in different bacterial species '''Please cite a paper or review here''' (See also <cite>BayerLabCellulosomeSystemsPage</cite>). In these systems, more than one scaffoldin interlocks with each other in various ways to produce a complex cellulosome architecture. At least one type of scaffoldin serves as a primary scaffoldin that incorporates the enzymes directly into the cellulosome complex. In each species, another type of scaffoldin attaches the cellulosome complex to the cell surface via a specialized module or sequence, designed for this purpose. In the complex cellulosome systems, the scaffoldin genes are organized into “multiple scaffoldin gene clusters” on the chromosome.
+To date, complex cellulosome systems have been described in different bacterial species (See also <cite>BayerLabCellulosomeSystemsPage cellulosome4 cellulosome6</cite>). In these systems, more than one scaffoldin interlocks with each other in various ways to produce a complex cellulosome architecture. At least one type of scaffoldin serves as a primary scaffoldin that incorporates the enzymes directly into the cellulosome complex. In each species, another type of scaffoldin attaches the cellulosome complex to the cell surface via a specialized module or sequence, designed for this purpose. In the complex cellulosome systems, the scaffoldin genes are organized into “multiple scaffoldin gene clusters” on the chromosome.
 [[File:Clostridium_cellulosome.jpg|500px|thumb|Schematic representation of ''C. thermocellum'' cellulosome components]]