PMID- 24241138
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20131119
LR  - 20211021
IS  - 0032-0935 (Print)
IS  - 0032-0935 (Linking)
VI  - 165
IP  - 3
DP  - 1985 Aug
TI  - A Chlamydomonas reinhardii mutant with catalytically and structurally altered 
      ribulose-5-phosphate kinase.
PG  - 340-7
LID - 10.1007/BF00392230 [doi]
AB  - The biochemical lesion in a light-sensitive, acetate-requiring Chlamydomonas 
      mutant was identified. This strain, designated rpk, exhibited photosynthetic 
      rates less than 3% of the wild-type. Analysis of photosynthetic products by 
      high-performance liquid chromatography demonstrated an accumulation of (14)C 
      label in pentose and hexose monophosphates. After 1 min of photosynthesis in 
      (14)CO2 these intermediates comprised 27.5% of the label in the mutant compared 
      with 8% in the wild-type. The mutant pheno-type was caused by a 20-fold reduction 
      in ribulose-5-phosphate (Ru5P)-kinase (EC 2.7.1.19) activity. The mutant 
      exhibited wild-type levels of ribulose-1,5-bisphosphate carboxylase (EC 
      4.1.1.39), fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) and transketolase (EC 
      2.2.1.1) indicating that the mutation specifically affected Ru5P kinase. In a 
      cross of the mutant with the wild-type, tetrad progeny segregated in a Mendelian 
      fashion (1:1) and light-sensitivity cosegregated with reduced Ru5P-kinase 
      activity and an acetate requirement for growth. Almost normal levels of 
      Ru5P-kinase protein were detected in the mutant by probing nitrocellulose 
      replicas of sodium dodecylsulfate-polyacrylamide gels with anti-Ru5P-kinase 
      antibody. The subunit size of the mutant enzyme, 42 kDa, was identical to that of 
      the wild-type. Isoelectric focusing of the native protein determined that the 
      mutant protein was altered, exhibiting a more acidic isoelectric point than the 
      wild-type protein. Thus, the molecular basis for the lesion affecting Ru5P-kinase 
      activity in mutant rpk is a charge alteration which results in a partially 
      impaired enzyme.
FAU - Salvucci, M E
AU  - Salvucci ME
AD  - Agricultural Research Service, U.S. Department of Agriculture, 1102 S. Goodwin 
      Ave., 61801, Urbana, IL, USA.
FAU - Ogren, W L
AU  - Ogren WL
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Planta
JT  - Planta
JID - 1250576
EDAT- 1985/08/01 00:00
MHDA- 1985/08/01 00:01
CRDT- 2013/11/19 06:00
PHST- 1984/12/21 00:00 [received]
PHST- 1985/03/25 00:00 [accepted]
PHST- 2013/11/19 06:00 [entrez]
PHST- 1985/08/01 00:00 [pubmed]
PHST- 1985/08/01 00:01 [medline]
AID - 10.1007/BF00392230 [doi]
PST - ppublish
SO  - Planta. 1985 Aug;165(3):340-7. doi: 10.1007/BF00392230.