Differential regulation of plastid mRNA stability. Progress report

Technical Report · Tue Sep 01 04:00:00 EDT 1992

OSTI ID:10176585

Our view of MRNA decay is that it is regulated by three interactive components: RNA structure, ribonucleases and RNAbinding proteins. We have used mutagenesis to study the role of RNA structure in regulating RNA decay rates, and to identify protein binding and endonuclease recognition sites. We have identified at least three endonuclease activities; one that cleaves psbA RNA; and two whose cleavage patterns with penD 3{prime}IR-RNA has been studied (endoC1 and endoC2). Additionally, we have continued to analyze the properties of the major RNA processing exoribonuclease. We have concentrated our efforts on three RNA-binding proteins. A 100 kd protein with properties suggestive of a mammalian RNP component has been purified. A protein of 55 kd that may also be an endonuclease has been partially purified. We have studied the interaction of a 29 kd protein with the pend stem/loop, and its role in RNA processing. Recently, we have used a novel gel shift/SDS-PAGE technique to identify new RNA-binding proteins that form complexes of as-yet unknown function.

• Research Organization: Boyce Thompson Inst. for Plant Research, Ithaca, NY (United States)
• Sponsoring Organization: USDOE, Washington, DC (United States)
• DOE Contract Number: FG02-90ER20015
• OSTI ID: 10176585
• Report Number(s): DOE/ER/20015--1; ON: DE92040451
• Country of Publication: United States
• Language: English

Related Subjects

09 BIOMASS FUELS
090800
550200
550400
553000
59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
AGRICULTURE AND FOOD TECHNOLOGY
AUTORADIOGRAPHY
BIOCHEMISTRY
BIOLOGICAL PATHWAYS
FRACTIONATION
GENE MUTATIONS
GENETIC ENGINEERING
GENETICS
MOLECULAR BIOLOGY
NUCLEOPROTEINS
PHOSPHORUS 32
PLANTS
PRODUCTION
PROGRESS REPORT
PROTEIN ENGINEERING
RNA PROCESSING