3 research outputs found
The Absence of Heat Shock Protein HSP101 Affects the Proteome of Mature and Germinating Maize Embryos
Maize heat shock protein HSP101 accumulates during embryo
maturation
and desiccation and persists at high levels during the first 24 h
following kernel imbibition in the absence of heat stress. This protein
has a known function in disaggregation of high molecular weight complexes
and has been proposed to be a translational regulator of specific
mRNAs. Here, a global proteomic approach was used to identify changes
in the maize proteome due to the absence of HSP101 in embryos from
mature-dry or 24 h-imbibed kernels. A total of 26 protein spots from
the mature dry embryo exhibited statistically significant expression
changes in the L10 inbred <i>hsp101</i> mutant (<i>hsp101-m5::Mu1</i>/<i>hsp101-m5::Mu1</i>) line as
compared to the corresponding wild type (<i>Hsp101</i>/<i>Hsp101</i>). Additional six spots reproducibly showed qualitative
changes between the mutant and wild-type mature and germinating embryos.
Several chaperones, translation-related proteins, actin, and enzymes
participating in cytokinin metabolism were identified in these spots
by tandem mass-spectrometry (MS). The proteomic changes partially
explain the altered root growth and architecture observed in young <i>hsp101</i> mutant seedlings. In addition, specific protein de
novo synthesis was altered in the 24 h-imbibed mutant embryos indicating
that maize HSP101 functions as both chaperone and translational regulator
during germination. Supporting this, HSP101 was found as part of Cap-binding
and translation initiation complexes during early kernel imbibition.
Overall, these findings expose the relevance of maize HSP101 for protein
synthesis and balance mechanisms during germination
The Absence of Heat Shock Protein HSP101 Affects the Proteome of Mature and Germinating Maize Embryos
Maize heat shock protein HSP101 accumulates during embryo
maturation
and desiccation and persists at high levels during the first 24 h
following kernel imbibition in the absence of heat stress. This protein
has a known function in disaggregation of high molecular weight complexes
and has been proposed to be a translational regulator of specific
mRNAs. Here, a global proteomic approach was used to identify changes
in the maize proteome due to the absence of HSP101 in embryos from
mature-dry or 24 h-imbibed kernels. A total of 26 protein spots from
the mature dry embryo exhibited statistically significant expression
changes in the L10 inbred <i>hsp101</i> mutant (<i>hsp101-m5::Mu1</i>/<i>hsp101-m5::Mu1</i>) line as
compared to the corresponding wild type (<i>Hsp101</i>/<i>Hsp101</i>). Additional six spots reproducibly showed qualitative
changes between the mutant and wild-type mature and germinating embryos.
Several chaperones, translation-related proteins, actin, and enzymes
participating in cytokinin metabolism were identified in these spots
by tandem mass-spectrometry (MS). The proteomic changes partially
explain the altered root growth and architecture observed in young <i>hsp101</i> mutant seedlings. In addition, specific protein de
novo synthesis was altered in the 24 h-imbibed mutant embryos indicating
that maize HSP101 functions as both chaperone and translational regulator
during germination. Supporting this, HSP101 was found as part of Cap-binding
and translation initiation complexes during early kernel imbibition.
Overall, these findings expose the relevance of maize HSP101 for protein
synthesis and balance mechanisms during germination
The Absence of Heat Shock Protein HSP101 Affects the Proteome of Mature and Germinating Maize Embryos
Maize heat shock protein HSP101 accumulates during embryo
maturation
and desiccation and persists at high levels during the first 24 h
following kernel imbibition in the absence of heat stress. This protein
has a known function in disaggregation of high molecular weight complexes
and has been proposed to be a translational regulator of specific
mRNAs. Here, a global proteomic approach was used to identify changes
in the maize proteome due to the absence of HSP101 in embryos from
mature-dry or 24 h-imbibed kernels. A total of 26 protein spots from
the mature dry embryo exhibited statistically significant expression
changes in the L10 inbred <i>hsp101</i> mutant (<i>hsp101-m5::Mu1</i>/<i>hsp101-m5::Mu1</i>) line as
compared to the corresponding wild type (<i>Hsp101</i>/<i>Hsp101</i>). Additional six spots reproducibly showed qualitative
changes between the mutant and wild-type mature and germinating embryos.
Several chaperones, translation-related proteins, actin, and enzymes
participating in cytokinin metabolism were identified in these spots
by tandem mass-spectrometry (MS). The proteomic changes partially
explain the altered root growth and architecture observed in young <i>hsp101</i> mutant seedlings. In addition, specific protein de
novo synthesis was altered in the 24 h-imbibed mutant embryos indicating
that maize HSP101 functions as both chaperone and translational regulator
during germination. Supporting this, HSP101 was found as part of Cap-binding
and translation initiation complexes during early kernel imbibition.
Overall, these findings expose the relevance of maize HSP101 for protein
synthesis and balance mechanisms during germination