YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism

Caplan, Avrom J.; Cyr, Douglas M.; Douglas, Michael G.

doi:10.1016/s0092-8674(05)80063-7

Cited by 265 publications

(254 citation statements)

References 55 publications

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“…Notably, loss of Ydj1 caused the most severe effects in the dependency of the critical size on growth rate. As Ydj1 is also involved in cell wall growth processes, such as protein translocation at the ER 35 , our data suggest that the key molecular device operating this correlation is at the interface between the cell cycle and cell growth machineries. In this regard, ribosome biogenesis activators Sfp1 and Sch9 also act as important negative regulators of Start 47 .…”

Section: Discussionmentioning

confidence: 70%

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

et al. 2012

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Budding yeast cells are assumed to trigger start and enter the cell cycle only after they attain a critical size set by external conditions. However, arguing against deterministic models of cell size control, cell volume at start displays great individual variability even under constant conditions. Here we show that cell size at start is robustly set at a single-cell level by the volume growth rate in G1, which explains the observed variability. We find that this growth-rate-dependent sizer is intimately hardwired into the start network and the Ydj1 chaperone is key for setting cell size as a function of the individual growth rate. mathematical modelling and experimental data indicate that a growth-rate-dependent sizer is sufficient to ensure size homeostasis and, as a remarkable advantage over a rigid sizer mechanism, it reduces noise in G1 length and provides an immediate solution for size adaptation to external conditions at a population level.

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Section: Discussionmentioning

confidence: 70%

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

et al. 2012

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“…These hsp70 proteins initially function to prevent aggregation of newly synthesized polypeptide chains (Ellis & van der Vies, 1991). Additional chaperones (Atencio & Yaffe, 1992;Caplan et al, 1992), including those that specifically recognize organellar targeting sequences (Ono & Tuboi, 1990;Murakami et al, 1992;Hachiya et al, 1993), may bind during or after translation. Some precursors will remain unfolded and aggregation prone as long as they are in the cytosol and thus will be associated with chaperones until translocation occurs (Chirico et al, 1988;Deshaies et al, 1988b;Murakami et al, 1988;Zimmermann et al, 1988;Waegemann et ai., 1990).…”

Section: Discussionmentioning

confidence: 99%

Import of cytochrome b₂ to the mitochondrial intermembrane space: The tightly folded heme‐binding domain makes import dependent upon matrix ATP

et al. 1993

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Cytochrome b2 is synthesized as a precursor in the cytoplasm and imported to the intermembrane space of yeast mitochondria. We show here that the precursor contains a tightly folded heme-binding domain and that translocation of this domain across the outer membrane requires ATP. Surprisingly, it is ATP in the mitochondrial matrix rather than external ATP that drives import of the heme-binding domain. When the folded structure of the heme-binding domain is disrupted by mutation or by urea denaturation, import and correct processing take place in ATP-depleted mitochondria. These results indicate that (1) cytochrome b2 reaches the intermembrane space without completely crossing the inner membrane, and (2) some precursors fold outside the mitochondria but remain translocation-competent, and import of these precursors in vitro does not require ATP-dependent cytosolic chaperone proteins.

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“…Ydjl has been shown to be involved in protein translocation into the ER and mitochondria (Atencio and Yaffe, 1992;Caplan et al, 1992b Fig. 3.…”

Section: (C) Construction Of the Yandl Xdjl Double-null Mutantmentioning

confidence: 99%

XDJ1, a gene encoding a novel non-essential DnaJ homologue from Saccharomyces cerevisiae

Schwarz¹,

Westermann²,

Caplan³

et al. 1994

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YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism

Cited by 265 publications

References 55 publications

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

Import of cytochrome b₂ to the mitochondrial intermembrane space: The tightly folded heme‐binding domain makes import dependent upon matrix ATP

XDJ1, a gene encoding a novel non-essential DnaJ homologue from Saccharomyces cerevisiae

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YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism

Cited by 265 publications

References 55 publications

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

Import of cytochrome b2 to the mitochondrial intermembrane space: The tightly folded heme‐binding domain makes import dependent upon matrix ATP

XDJ1, a gene encoding a novel non-essential DnaJ homologue from Saccharomyces cerevisiae

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Import of cytochrome b₂ to the mitochondrial intermembrane space: The tightly folded heme‐binding domain makes import dependent upon matrix ATP