Polypeptide composition of bacterial cyclic diguanylic acid-dependent cellulose synthase and the occurrence of immunologically crossreacting proteins in higher plants

Journal Article · Sat Jun 15 00:00:00 EDT 1991 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

DOI:https://doi.org/10.1073/pnas.88.12.5472· OSTI ID:6100359

Mayer, R; Ross, P; Weinhouse, H; Amikam, D; Volman, G; Ohana, P; Benziman, M ^[1]; Calhoon, R D; Wong, Hing C; Emerick, A W ^[2]

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1. Hebrew Univ., Jerusalem (Israel)
2. Cetus Corp., Emeryville, CA (United States)

To comprehend the catalytic and regulatory mechanism of the cyclic diguanylic acid (c-di-GMP)-dependent cellulose synthase of Acetobacter xylinum and its relatedness to similar enzymes in other organisms, the structure of this enzyme was analyzed at the polypeptide level. The enzyme, purified 350-fold by enzyme-product entrapment, contains three major peptides (90, 67, and 54 kDa), which, based on direct photoaffinity and immunochemical labeling and amino acid sequence analysis, are constituents of the native cellulose synthase. Labeling of purified synthase with either ({sup 32}P)c-di-GMP or ({alpha}-{sup 32}P)UDP-glucose indicates that activator- and substrate-specific binding sites are most closely associated with the 67- and 54-kDa peptides, respectively, whereas marginal photolabeling is detected in the 90-k-Da peptide. However, antibodies raised against a protein derived from the cellulose synthase structural gene (bcsB) specifically label all three peptides. The authors suggest that the structurally related 67- and 54-kDa peptides are fragments proteolytically derived from the 90-kDa peptide encoded by bcsB. The anti-cellulose synthase antibodies crossreact with a similar set of peptides derived from other cellulose-producing microorganisms and plants such as Agrobacterium tumefaciens, Rhizobium leguminosarum, mung bean, peas, barley, and cotton. The occurrence of such cellulose synthase-like structures in plant species suggests that a common enzymatic mechanism for cellulose biogenesis is employed throughout nature.

• OSTI ID: 6100359
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:12; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
CELLULOSE
BIOSYNTHESIS
LIGASES
AMINO ACID SEQUENCE
BIOCHEMICAL REACTION KINETICS
ELECTROPHORESIS
GUANYLIC ACID
IMMUNOLOGY
PHOSPHORUS 32
POLYPEPTIDES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBOHYDRATES
DAYS LIVING RADIOISOTOPES
ENZYMES
ISOTOPES
KINETICS
LIGHT NUCLEI
MOLECULAR STRUCTURE
NUCLEI
NUCLEOTIDES
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PEPTIDES
PHOSPHORUS ISOTOPES
POLYSACCHARIDES
PROTEINS
RADIOISOTOPES
REACTION KINETICS
SACCHARIDES
SYNTHESIS
550201* - Biochemistry- Tracer Techniques