Biosynthesis and degradation of storage protein in spores of the fungus Botryodiplodia theobromae.

G. R. Petersen, K. R. Dahlberg, J. L. Van Etten

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Muiridin, a spore-specific protein of the fungus Botryodiplodia theobromae, comprises about 25% of the mature pycnidiospore protein. It has an apparent molecular weight of 16,000 to 17,000 and is rich in glutamine, asparagine, and arginine. Muiridin is synthesized in developing spores via a precursor with an apparent molecular weight of 24,000. Two other polypeptides present in young developing spores with apparent molecular weights of 18,000 and 15,000 are immunologically related to muiridin. We propose a pathway for muiridin synthesis. Muiridin is actively degraded during the germination of spores from 30-day-old cultures. This degradation is independent of exogenous amino acids in the germination medium. In contrast, glutamine and, to a lesser extent, asparagine partially inhibit the degradation of muiridin during germination of spores from 7-day-old cultures.

Original languageEnglish (US)
Pages (from-to)601-606
Number of pages6
JournalJournal of bacteriology
Volume155
Issue number2
StatePublished - Aug 1 1983

Fingerprint

Spores
Proteolysis
Fungi
Germination
Molecular Weight
Asparagine
Glutamine
Arginine
Proteins
Amino Acids
Peptides

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Biosynthesis and degradation of storage protein in spores of the fungus Botryodiplodia theobromae. / Petersen, G. R.; Dahlberg, K. R.; Van Etten, J. L.

In: Journal of bacteriology, Vol. 155, No. 2, 01.08.1983, p. 601-606.

Research output: Contribution to journalArticle

@article{941e5c487af84d51ab40ee09f757fe2c,
title = "Biosynthesis and degradation of storage protein in spores of the fungus Botryodiplodia theobromae.",
abstract = "Muiridin, a spore-specific protein of the fungus Botryodiplodia theobromae, comprises about 25{\%} of the mature pycnidiospore protein. It has an apparent molecular weight of 16,000 to 17,000 and is rich in glutamine, asparagine, and arginine. Muiridin is synthesized in developing spores via a precursor with an apparent molecular weight of 24,000. Two other polypeptides present in young developing spores with apparent molecular weights of 18,000 and 15,000 are immunologically related to muiridin. We propose a pathway for muiridin synthesis. Muiridin is actively degraded during the germination of spores from 30-day-old cultures. This degradation is independent of exogenous amino acids in the germination medium. In contrast, glutamine and, to a lesser extent, asparagine partially inhibit the degradation of muiridin during germination of spores from 7-day-old cultures.",
author = "Petersen, {G. R.} and Dahlberg, {K. R.} and {Van Etten}, {J. L.}",
year = "1983",
month = "8",
day = "1",
language = "English (US)",
volume = "155",
pages = "601--606",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "2",

}

TY - JOUR

T1 - Biosynthesis and degradation of storage protein in spores of the fungus Botryodiplodia theobromae.

AU - Petersen, G. R.

AU - Dahlberg, K. R.

AU - Van Etten, J. L.

PY - 1983/8/1

Y1 - 1983/8/1

N2 - Muiridin, a spore-specific protein of the fungus Botryodiplodia theobromae, comprises about 25% of the mature pycnidiospore protein. It has an apparent molecular weight of 16,000 to 17,000 and is rich in glutamine, asparagine, and arginine. Muiridin is synthesized in developing spores via a precursor with an apparent molecular weight of 24,000. Two other polypeptides present in young developing spores with apparent molecular weights of 18,000 and 15,000 are immunologically related to muiridin. We propose a pathway for muiridin synthesis. Muiridin is actively degraded during the germination of spores from 30-day-old cultures. This degradation is independent of exogenous amino acids in the germination medium. In contrast, glutamine and, to a lesser extent, asparagine partially inhibit the degradation of muiridin during germination of spores from 7-day-old cultures.

AB - Muiridin, a spore-specific protein of the fungus Botryodiplodia theobromae, comprises about 25% of the mature pycnidiospore protein. It has an apparent molecular weight of 16,000 to 17,000 and is rich in glutamine, asparagine, and arginine. Muiridin is synthesized in developing spores via a precursor with an apparent molecular weight of 24,000. Two other polypeptides present in young developing spores with apparent molecular weights of 18,000 and 15,000 are immunologically related to muiridin. We propose a pathway for muiridin synthesis. Muiridin is actively degraded during the germination of spores from 30-day-old cultures. This degradation is independent of exogenous amino acids in the germination medium. In contrast, glutamine and, to a lesser extent, asparagine partially inhibit the degradation of muiridin during germination of spores from 7-day-old cultures.

UR - http://www.scopus.com/inward/record.url?scp=0020808094&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020808094&partnerID=8YFLogxK

M3 - Article

C2 - 6874639

AN - SCOPUS:0020808094

VL - 155

SP - 601

EP - 606

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 2

ER -