Processing of cellulose synthase (AcsAB) from Gluconacetobacter hansenii 23769

Prashanti R. Iyer; Yu An Liu; Ying Deng; John B. McManus; Teh Hui Kao; Ming Tien

doi:10.1016/j.abb.2012.12.002

Processing of cellulose synthase (AcsAB) from Gluconacetobacter hansenii 23769

Prashanti R. Iyer, Yu An Liu, Ying Deng, John B. McManus, Teh Hui Kao, Ming Tien

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

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Abstract

The cellulose synthase protein (AcsAB) is encoded by a single gene in Gluconacetobacter hansenii ATCC 23769. We have examined the processing pattern of this enzyme and the localization of the cleavage products by heterologously expressing the truncated portions of the AcsAB protein and using specific antibodies generated against these regions. We found that the AcsAB protein is processed into three polypeptide subunits of molecular masses 46 kDa, 34 kDa and 95 kDa. The 46 kDa polypeptide (AcsA_cat) harbors the conserved glycosyltransferase domain and hence contains the catalytic subunit of the enzyme. This polypeptide is localized in the cytoplasmic membrane. The 34 kDa polypeptide (AcsA_reg) is the regulatory subunit with the cyclic diGMP-binding PilZ domain. This polypeptide is largely cytoplasmic. The 95 kDa subunit (AcsB) is of unknown function and contains a predicted signal peptide at its N-terminus. This subunit is localized in the outer membrane. In addition to this, we have also localized the AcsC protein in the outer membrane, confirming its predicted localization based on the OM-signal sequence at its N-terminus.

Original language	English (US)
Pages (from-to)	92-98
Number of pages	7
Journal	Archives of Biochemistry and Biophysics
Volume	529
Issue number	2
DOIs	https://doi.org/10.1016/j.abb.2012.12.002
State	Published - Jan 15 2013

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology

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title = "Processing of cellulose synthase (AcsAB) from Gluconacetobacter hansenii 23769",

abstract = "The cellulose synthase protein (AcsAB) is encoded by a single gene in Gluconacetobacter hansenii ATCC 23769. We have examined the processing pattern of this enzyme and the localization of the cleavage products by heterologously expressing the truncated portions of the AcsAB protein and using specific antibodies generated against these regions. We found that the AcsAB protein is processed into three polypeptide subunits of molecular masses 46 kDa, 34 kDa and 95 kDa. The 46 kDa polypeptide (AcsAcat) harbors the conserved glycosyltransferase domain and hence contains the catalytic subunit of the enzyme. This polypeptide is localized in the cytoplasmic membrane. The 34 kDa polypeptide (AcsAreg) is the regulatory subunit with the cyclic diGMP-binding PilZ domain. This polypeptide is largely cytoplasmic. The 95 kDa subunit (AcsB) is of unknown function and contains a predicted signal peptide at its N-terminus. This subunit is localized in the outer membrane. In addition to this, we have also localized the AcsC protein in the outer membrane, confirming its predicted localization based on the OM-signal sequence at its N-terminus.",

author = "Iyer, {Prashanti R.} and Liu, {Yu An} and Ying Deng and McManus, {John B.} and Kao, {Teh Hui} and Ming Tien",

note = "Funding Information: This material is based upon work supported as part of The Center for LignoCellulose Structure and Formation, an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences under Award Number DE-SC0001090. We thank D.J. Wasilko for performing the cellulose synthase activity assays. We acknowledge one of the reviewers for examining results with G. hansenii ATCC53582 to identify the cleavage site.",

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T1 - Processing of cellulose synthase (AcsAB) from Gluconacetobacter hansenii 23769

AU - Iyer, Prashanti R.

AU - Liu, Yu An

AU - Deng, Ying

AU - McManus, John B.

AU - Kao, Teh Hui

AU - Tien, Ming

N1 - Funding Information: This material is based upon work supported as part of The Center for LignoCellulose Structure and Formation, an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences under Award Number DE-SC0001090. We thank D.J. Wasilko for performing the cellulose synthase activity assays. We acknowledge one of the reviewers for examining results with G. hansenii ATCC53582 to identify the cleavage site.

PY - 2013/1/15

Y1 - 2013/1/15

N2 - The cellulose synthase protein (AcsAB) is encoded by a single gene in Gluconacetobacter hansenii ATCC 23769. We have examined the processing pattern of this enzyme and the localization of the cleavage products by heterologously expressing the truncated portions of the AcsAB protein and using specific antibodies generated against these regions. We found that the AcsAB protein is processed into three polypeptide subunits of molecular masses 46 kDa, 34 kDa and 95 kDa. The 46 kDa polypeptide (AcsAcat) harbors the conserved glycosyltransferase domain and hence contains the catalytic subunit of the enzyme. This polypeptide is localized in the cytoplasmic membrane. The 34 kDa polypeptide (AcsAreg) is the regulatory subunit with the cyclic diGMP-binding PilZ domain. This polypeptide is largely cytoplasmic. The 95 kDa subunit (AcsB) is of unknown function and contains a predicted signal peptide at its N-terminus. This subunit is localized in the outer membrane. In addition to this, we have also localized the AcsC protein in the outer membrane, confirming its predicted localization based on the OM-signal sequence at its N-terminus.

AB - The cellulose synthase protein (AcsAB) is encoded by a single gene in Gluconacetobacter hansenii ATCC 23769. We have examined the processing pattern of this enzyme and the localization of the cleavage products by heterologously expressing the truncated portions of the AcsAB protein and using specific antibodies generated against these regions. We found that the AcsAB protein is processed into three polypeptide subunits of molecular masses 46 kDa, 34 kDa and 95 kDa. The 46 kDa polypeptide (AcsAcat) harbors the conserved glycosyltransferase domain and hence contains the catalytic subunit of the enzyme. This polypeptide is localized in the cytoplasmic membrane. The 34 kDa polypeptide (AcsAreg) is the regulatory subunit with the cyclic diGMP-binding PilZ domain. This polypeptide is largely cytoplasmic. The 95 kDa subunit (AcsB) is of unknown function and contains a predicted signal peptide at its N-terminus. This subunit is localized in the outer membrane. In addition to this, we have also localized the AcsC protein in the outer membrane, confirming its predicted localization based on the OM-signal sequence at its N-terminus.

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Processing of cellulose synthase (AcsAB) from Gluconacetobacter hansenii 23769

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