Structural divergence between the two subgroups of P5 ATPases

Danny Mollerup Sørensen; Morten Jeppe Buch-Pedersen; Michael Broberg Palmgren

doi:10.1016/j.bbabio.2010.04.010

Structural divergence between the two subgroups of P5 ATPases

Danny Mollerup Sørensen, Morten Jeppe Buch-Pedersen, Michael Broberg Palmgren

23 Citations (Scopus)

Abstract

Evolution of P5 type ATPases marks the origin of eukaryotes but still they remain the least characterized pumps in the superfamily of P-type ATPases. Phylogenetic analysis of available sequences suggests that P5 ATPases should be divided into at least two subgroups, P5A and P5B. P5A ATPases have been identified in the endoplasmic reticulum and seem to have basic functions in protein maturation and secretion. P5B ATPases localize to vacuolar/lysosomal or apical membranes and in animals play a role in hereditary neuronal diseases. Here we have used a bioinformatical approach to identify differences in the primary sequences between the two subgroups. P5A and P5B ATPases appear have a very different membrane topology from other P-type ATPases with two and one, respectively, additional transmembrane segments inserted in the N-terminal end. Based on conservation of residues in the transmembrane region, the two P5 subgroups most likely have different substrate specificities although these cannot be predicted from their sequences. Furthermore, sequence differences between P5A and P5B ATPases are identified in the catalytic domains that could influence key kinetic properties differentially. Together these findings indicate that P5A and P5B ATPases are structurally and functionally different.

Original language	English
Journal	BBA General Subjects
Volume	1797
Issue number	6-7
Pages (from-to)	846-855
Number of pages	10
ISSN	0304-4165
DOIs	https://doi.org/10.1016/j.bbabio.2010.04.010
Publication status	Published - Jun 2010

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10.1016/j.bbabio.2010.04.010

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@article{a8bf75ee2b6549e99c7114e8c5cd15ef,

title = "Structural divergence between the two subgroups of P5 ATPases",

abstract = "Evolution of P5 type ATPases marks the origin of eukaryotes but still they remain the least characterized pumps in the superfamily of P-type ATPases. Phylogenetic analysis of available sequences suggests that P5 ATPases should be divided into at least two subgroups, P5A and P5B. P5A ATPases have been identified in the endoplasmic reticulum and seem to have basic functions in protein maturation and secretion. P5B ATPases localize to vacuolar/lysosomal or apical membranes and in animals play a role in hereditary neuronal diseases. Here we have used a bioinformatical approach to identify differences in the primary sequences between the two subgroups. P5A and P5B ATPases appear have a very different membrane topology from other P-type ATPases with two and one, respectively, additional transmembrane segments inserted in the N-terminal end. Based on conservation of residues in the transmembrane region, the two P5 subgroups most likely have different substrate specificities although these cannot be predicted from their sequences. Furthermore, sequence differences between P5A and P5B ATPases are identified in the catalytic domains that could influence key kinetic properties differentially. Together these findings indicate that P5A and P5B ATPases are structurally and functionally different. ",

author = "S{\o}rensen, {Danny Mollerup} and Buch-Pedersen, {Morten Jeppe} and Palmgren, {Michael Broberg}",

year = "2010",

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doi = "10.1016/j.bbabio.2010.04.010",

language = "English",

volume = "1797",

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journal = "B B A - General Subjects",

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TY - JOUR

T1 - Structural divergence between the two subgroups of P5 ATPases

AU - Sørensen, Danny Mollerup

AU - Buch-Pedersen, Morten Jeppe

AU - Palmgren, Michael Broberg

PY - 2010/6

Y1 - 2010/6

N2 - Evolution of P5 type ATPases marks the origin of eukaryotes but still they remain the least characterized pumps in the superfamily of P-type ATPases. Phylogenetic analysis of available sequences suggests that P5 ATPases should be divided into at least two subgroups, P5A and P5B. P5A ATPases have been identified in the endoplasmic reticulum and seem to have basic functions in protein maturation and secretion. P5B ATPases localize to vacuolar/lysosomal or apical membranes and in animals play a role in hereditary neuronal diseases. Here we have used a bioinformatical approach to identify differences in the primary sequences between the two subgroups. P5A and P5B ATPases appear have a very different membrane topology from other P-type ATPases with two and one, respectively, additional transmembrane segments inserted in the N-terminal end. Based on conservation of residues in the transmembrane region, the two P5 subgroups most likely have different substrate specificities although these cannot be predicted from their sequences. Furthermore, sequence differences between P5A and P5B ATPases are identified in the catalytic domains that could influence key kinetic properties differentially. Together these findings indicate that P5A and P5B ATPases are structurally and functionally different.

AB - Evolution of P5 type ATPases marks the origin of eukaryotes but still they remain the least characterized pumps in the superfamily of P-type ATPases. Phylogenetic analysis of available sequences suggests that P5 ATPases should be divided into at least two subgroups, P5A and P5B. P5A ATPases have been identified in the endoplasmic reticulum and seem to have basic functions in protein maturation and secretion. P5B ATPases localize to vacuolar/lysosomal or apical membranes and in animals play a role in hereditary neuronal diseases. Here we have used a bioinformatical approach to identify differences in the primary sequences between the two subgroups. P5A and P5B ATPases appear have a very different membrane topology from other P-type ATPases with two and one, respectively, additional transmembrane segments inserted in the N-terminal end. Based on conservation of residues in the transmembrane region, the two P5 subgroups most likely have different substrate specificities although these cannot be predicted from their sequences. Furthermore, sequence differences between P5A and P5B ATPases are identified in the catalytic domains that could influence key kinetic properties differentially. Together these findings indicate that P5A and P5B ATPases are structurally and functionally different.

U2 - 10.1016/j.bbabio.2010.04.010

DO - 10.1016/j.bbabio.2010.04.010

M3 - Journal article

C2 - 20416272

SN - 0304-4165

VL - 1797

SP - 846

EP - 855

JO - B B A - General Subjects

JF - B B A - General Subjects

IS - 6-7

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