Secretion of α-Amylase from
            <i>Pseudoalteromonas haloplanktis</i>
            TAB23: Two Different Pathways in Different Hosts

Tutino, Maria Luisa; Parrilli, Ermenegilda; Giaquinto, Laura; Duilio, Angela; Sannia, Giovanni; Feller, Georges; Marino, Gennaro

doi:10.1128/jb.184.20.5814-5817.2002

Cited by 31 publications

(34 citation statements)

References 19 publications

(21 reference statements)

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“…This provides only a small glimpse into the exceptional adaptation of the microbiota to the Antarctic environment. The Pseudoalteromonas isolates in particular showed great potential for bioprospecting of all screened enzymatic activities, a result that agrees with those from previous studies (Holmströ m & Kjelleberg 1999;Hoyoux et al 2001;Truong et al 2001;Tutino et al 2002;Zeng et al 2006). Beyond the biotechnological potential, the high proportion of isolates belonging to the genus Pseudoalteromonas and the versatile hydrolytic activities detected in this group also suggest that these organisms may play an important role in polymer hydrolysis in cold environments.…”

Section: Discussionsupporting

confidence: 80%

Culturable heterotrophic bacteria from Potter Cove, Antarctica, and their hydrolytic enzymes production

Tropeano¹,

Coria²,

Turjanski³

et al. 2012

Polar Research

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Affiliations of the dominant culturable bacteria isolated from Potter Cove, South Shetland Islands, Antarctica, were investigated together with their production of cold-active hydrolytic enzymes. A total of 189 aerobic heterotrophic bacterial isolates were obtained at 4°C and sorted into 63 phylotypes based on their amplified ribosomal DNA restriction analysis profiles. The sequencing of the 16S rRNA genes of representatives from each phylotype showed that the isolates belong to the phyla Proteobacteria (classes Alpha- and Gamma-proteobacteria), Bacteroidetes (class Flavobacteria), Actinobacteria (class Actinobacteria) and Firmicutes (class Bacilli). The predominant culturable group in the site studied belongs to the class Gammaproteobacteria, with 65 isolates affiliated to the genus Pseudoalteromonas and 58 to Psychrobacter. Among the 189 isolates screened, producers of amylases (9.5%), pectinases (22.8%), cellulases (14.8%), CM-cellulases (25.4%), xylanases (20.1%) and proteases (44.4%) were detected. More than 25% of the isolates produced at least one extracellular enzyme, with some of them producing up to six of the tested extracellular enzymatic activities. These results suggest that a high culturable bacterial diversity is present in Potter Cove and that this place represents a promising source of biomolecules

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Section: Discussionsupporting

confidence: 80%

Culturable heterotrophic bacteria from Potter Cove, Antarctica, and their hydrolytic enzymes production

Tropeano¹,

Coria²,

Turjanski³

et al. 2012

Polar Research

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“…This also gives evidence of the versatility of the culturable microbiota from Potter Cove to take advantage of the nutrient sources, which are sometimes scarce in the Antarctic. In fact, Pseudoalteromonas isolates showed a great potential for the bioprospection of a great number of enzymes, in accor− dance with other reports (Holmström and Kjelleberg 1999;Truong et al 2001;Tutino et al 2002;Van Petegem et al 2003;Zeng et al 2006). The versatile hydrolytic capacity exhibited by this genus and its remarkable abundance among the producers of cold enzymes suggest its relevance to the recycling of organic matter.…”

Section: Discussionsupporting

confidence: 73%

Extracellular hydrolytic enzyme production by proteolytic bacteria from the Antarctic

Tropeano¹,

Vázquez²,

Coria³

et al. 2013

Polish Polar Research

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Cold−adapted marine bacteria producing extracellular hydrolytic enzymes are important for their industrial application and play a key role in degradation of particulate or− ganic matter in their natural environment. In this work, members of a previously−obtained protease−producing bacterial collection isolated from different marine sources from Potter Cove (King George Island, South Shetlands) were taxonomically identified and screened for their ability to produce other economically relevant enzymes. Eighty−eight proteolytic bacterial isolates were grouped into 25 phylotypes based on their Amplified Ribosomal DNA Restriction Analysis profiles. The sequencing of the 16S rRNA genes from represen− tative isolates of the phylotypes showed that the predominant culturable protease−producing bacteria belonged to the class Gammaproteobacteria and were affiliated to the genera Pseu− domonas, Shewanella, Colwellia, and Pseudoalteromonas, the latter being the predominant group (64% of isolates). In addition, members of the classes Actinobacteria, Bacilli and Flavobacteria were found. Among the 88 isolates screened we detected producers of amylases (21), pectinases (67), cellulases (53), CM−cellulases (68), xylanases (55) and agarases (57). More than 85% of the isolates showed at least one of the extracellular enzy− matic activities tested, with some of them producing up to six extracellular enzymes. Our results confirmed that using selective conditions to isolate producers of one extracellular Pol. Polar Res. 34 (3): 253-267, 2013Res. 34 (3): 253-267, vol. 34, no. 3, pp. 253-267, 2013 doi: 10.2478/popore−2013−0014 Unauthenticated Download Date | 5/10/18 5:03 PM enzyme activity increases the probability of recovering bacteria that will also produce addi− tional extracellular enzymes. This finding establishes a starting point for future programs oriented to the prospecting for biomolecules in Antarctica.

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“…The development of genetic tools for manipulation of Antarctica bacteria (Parrilli et al, 2008a) allowed us to demonstrate that the C-terminal propeptide is not mandatory for a-amylase recombinant secretion either in the source strain or in the related strain P. haloplanktis TAC125 (Tutino et al, 2002). Indeed, the propeptide can be replaced by other protein domains without affecting the secretion of the chimeric proteins (Cusano et al, 2006b;Parrilli et al, 2008b).…”

Section: Discussionmentioning

confidence: 99%

“…Although the C-terminal propeptide sequence is not homologous to that of b-autotransporters (Henderson et al, 2004), in a previous paper (Feller et al, 1998) it was suggested that it may function as a protein secretion helper when amylase is produced in Escherichia coli. However, different results were obtained when the secretion of recombinant a-amylase and its truncated version, devoid of the C-terminal domain, was investigated either in the enzyme source strain, P. haloplanktis TAB23, or in another Antarctic bacterium, P. haloplanktis TAC125 (Tutino et al, 2002). It was demonstrated that the Cterminal propeptide is not mandatory for a-amylase secretion and that the presence of the C-terminal domain does not interfere either with the secretion kinetics or with the maximal secretion and production yield (Tutino et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…a-Amylase secretion was studied in P. haloplanktis TAC125. Several reasons prompted us to use this bacterium as recombinant host: (i) it is the first Antarctic micro-organism whose genome has been sequenced and annotated (Médigue et al, 2005); (ii) in this bacterium, recombinant a-amylase secretion occurs in a way similar to that in the source strain (Tutino et al, 2001(Tutino et al, , 2002; (iii) P. haloplanktis TAC125 is devoid of endogenous a-amylase activity (Tutino et al, 2001); and (iv) the cold-adapted a-amylase was successfully used as secretion carrier in a cold gene-expression system for secretion of heterologous proteins in P. haloplanktis TAC125 (Cusano et al, 2006b;Parrilli et al, 2008b).…”

Section: Introductionmentioning

confidence: 99%

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PssA is required for α-amylase secretion in Antarctic Pseudoalteromonas haloplanktis

et al. 2010

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Extracellular protein secretion is an essential feature in bacterial physiology. The ability to efficiently secrete diverse hydrolytic enzymes represents a key nutritional strategy for all bacteria, including micro-organisms living in extreme and hostile habitats, such as cold environments. However, little is known about protein secretion mechanisms in psychrophilic bacteria. In this study, the recombinant secretion of a cold-adapted α-amylase in the Antarctic Gram-negative Pseudoalteromonas haloplanktis TAC125 was investigated. By a combination of several molecular techniques, the function of the pssA gene was related to α-amylase secretion in this psychrophilic bacterium. Deletion of the pssA gene completely abolished amylase secretion without affecting the extracellular targeting of other substrates mediated by canonical secretion systems. The pssA gene product, PssA, is a multidomain lipoprotein, predicted to be localized in the bacterial outer membrane, and displaying three TPR (tetratricopeptide repeat) domains and two LysM modules. Based on functional annotation of these domains, combined with the experimental results reported herein, we suggest a role for PssA as a molecular adaptor, in charge of recruiting other cellular components required for specific α-amylase secretion. To the best of our knowledge, no proteins exhibiting the same domain organization have previously been linked to protein secretion.

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Secretion of α-Amylase from Pseudoalteromonas haloplanktis TAB23: Two Different Pathways in Different Hosts

Cited by 31 publications

References 19 publications

Culturable heterotrophic bacteria from Potter Cove, Antarctica, and their hydrolytic enzymes production

Culturable heterotrophic bacteria from Potter Cove, Antarctica, and their hydrolytic enzymes production

Extracellular hydrolytic enzyme production by proteolytic bacteria from the Antarctic

PssA is required for α-amylase secretion in Antarctic Pseudoalteromonas haloplanktis

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